2ERH - JenaLib

Title :   CRYSTAL STRUCTURE OF THE E7_G/IM7_G COMPLEX; A DESIGNED INTERFACE BETWEEN THE COLICIN E7 DNASE AND THE IM7 IMMUNITY PROTEIN

Authors :   L. A. Joachimiak, T. Kortemme, B. L. Stoddard, D. Baker

Date :   24 Oct 05 (Deposition) - 25 Jul 06 (Release) - 24 Feb 09 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   2.00

Chains :   Asym./Biol. Unit : A,B

Keywords :   Computational Design, Redesigned Protein-Protein Interface, Hydrogen Bond Network, Specificity, Molecular Recognition, Protein Complex, Hydrolase/Hydrolase Inhibitor Complex (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   L. A. Joachimiak, T. Kortemme, B. L. Stoddard, D. Baker
Computational Design Of A New Hydrogen Bond Network And At Least A 300-Fold Specificity Switch At A Protein-Protein Interface.
J. Mol. Biol. V. 361 195 2006
PubMed-ID: 16831445 | Reference-DOI: 10.1016/J.JMB.2006.05.022
(for further references see the PDB file header)

Compounds

Molecule 1 - COLICIN E7 IMMUNITY PROTEIN
	Chains	:	A
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Plasmid	:	PQE-30
	Expression System Strain	:	SG13009
	Expression System Taxid	:	562
	Expression System Vector Type	:	PLASMID
	Gene	:	IMM, CEIE7
	Mutation	:	YES
	Organism Scientific	:	ESCHERICHIA COLI
	Organism Taxid	:	562
	Synonym	:	IMME7, MICROCIN E7 IMMUNITY PROTEIN

Molecule 2 - COLICIN E7
	Chains	:	B
	EC Number	:	3.1.-.-
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Taxid	:	562
	Expression System Vector Type	:	PLASMID
	Gene	:	COLE7, CEA
	Mutation	:	YES
	Organism Scientific	:	ESCHERICHIA COLI
	Organism Taxid	:	562

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (0, 0)

Sites (0, 0)

SS Bonds (0, 0)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (0, 0)

Exons (0, 0)

Sequences/Alignments

Asymmetric/Biological Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
	Number of residues per labelling interval =
	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
	(details for a mapped element are shown in a popup box when the mouse pointer rests over it)

Chain A from PDB  Type:PROTEIN  Length:87
 aligned with IMM7_ECOLX | Q03708 from UniProtKB/Swiss-Prot  Length:87

    Alignment length:87
                                    10        20        30        40        50        60        70        80       
           IMM7_ECOLX     1 MELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQG  87
               SCOP domains --------------------------------------------------------------------------------------- SCOP domains
               CATH domains 2erhA00 A:1-87  [code=1.10.1200.20, no name defined]                                    CATH domains
               Pfam domains --------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .....hhhhhhhhhhhhhhhhhhhhh....hhhhhhhhhhhhhhhh....hhhhhh.......hhhhhhhhhhhhhhhh........ Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------- Transcript
                 2erh A   1 MELKNSISDYTEAEFVQLLKEIEKENVAATDDVLYVLLEHFVKITEHPDGQDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQG  87
                                    10        20        30        40        50        60        70        80

Chain B from PDB  Type:PROTEIN  Length:127
 aligned with CEA7_ECOLX | Q47112 from UniProtKB/Swiss-Prot  Length:576

    Alignment length:127
                                   456       466       476       486       496       506       516       526       536       546       556       566       
           CEA7_ECOLX   447 RNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEVSKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKRTSFELHHEKPISQNGGVYDMDNISVVTPKRHIDIH 573
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains 2erhB00 B:447-573 Colicin e7 immunity protein. Chain B                                                                          CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ....ee.....................ee.hhhhhhhhh..ee.hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh......hhhhh.......eeee...............eeeehhhhhhhhh Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2erh B 447 RNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEVSKDPELSKQFSRTQNDRMKVGRAPQTRTQDVSGKRQSFELHHEKPISQNGGVYDMDNISVVTPKRHIDIH 573
                                   456       466       476       486       496       506       516       526       536       546       556       566

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

Classification and Annotation

SCOP Domains (0, 0)

CATH Domains (2, 2)

Pfam Domains (0, 0)

Gene Ontology (12, 13)

Asymmetric/Biological Unit(hide GO term definitions)

Chain A (IMM7_ECOLX | Q03708)

molecular function
	GO:0005515	protein binding	Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
	GO:0015643	toxic substance binding	Interacting selectively and non-covalently with a toxic substance, a poisonous substance that causes damage to biological systems.
biological process
	GO:0030153	bacteriocin immunity	A process that mediates resistance to a bacteriocin: any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.

Chain B (CEA7_ECOLX | Q47112)

molecular function
	GO:0004519	endonuclease activity	Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks.
	GO:0016787	hydrolase activity	Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
	GO:0046872	metal ion binding	Interacting selectively and non-covalently with any metal ion.
	GO:0004518	nuclease activity	Catalysis of the hydrolysis of ester linkages within nucleic acids.
	GO:0005515	protein binding	Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
biological process
	GO:0019835	cytolysis	The rupture of cell membranes and the loss of cytoplasm.
	GO:0042742	defense response to bacterium	Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
	GO:0090305	nucleic acid phosphodiester bond hydrolysis	The nucleic acid metabolic process in which the phosphodiester bonds between nucleotides are cleaved by hydrolysis.
	GO:0009405	pathogenesis	The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
cellular component
	GO:0005727	extrachromosomal circular DNA	Circular DNA structures that are not part of a chromosome.

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Description