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1gpq

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Revision as of 11:00, 25 December 2014

STRUCTURE OF IVY COMPLEXED WITH ITS TARGET, HEWL

Structural highlights

1gpq is a 4 chain structure with sequence from Escherichia coli k-12 and Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	132l, 193l, 194l, 1a2y, 1aki, 1at5, 1at6, 1azf, 1b0d, 1b2k, 1bgi, 1bhz, 1bvk, 1bvx, 1bwh, 1bwi, 1bwj, 1c08, 1c10, 1dpw, 1dpx, 1dqj, 1e8l, 1f0w, 1f10, 1f3j, 1fdl, 1flq, 1flu, 1flw, 1fly, 1fn5, 1g7h, 1g7i, 1g7j, 1g7l, 1g7m, 1h6m, 1h87, 1hc0, 1hel, 1hem, 1hen, 1heo, 1hep, 1heq, 1her, 1hew, 1hf4, 1hsw, 1hsx, 1ic4, 1ic5, 1ic7, 1iee, 1io5, 1ioq, 1ior, 1ios, 1iot, 1ja2, 1ja4, 1ja6, 1ja7, 1jpo, 1jto, 1kip, 1kiq, 1kir, 1kxw, 1kxx, 1kxy, 1lcn, 1lkr, 1lks, 1lma, 1lpi, 1lsa, 1lsb, 1lsc, 1lsd, 1lse, 1lsf, 1lsg, 1lsm, 1lsn, 1lsy, 1lsz, 1lyo, 1lys, 1lyz, 1lz8, 1lz9, 1lza, 1lzb, 1lzc, 1lzd, 1lze, 1lzg, 1lzh, 1lzn, 1lzt, 1mel, 1mlc, 1qio, 1qtk, 1rcm, 1rfp, 1uco, 1uia, 1uib, 1uic, 1uid, 1uie, 1uif, 1uig, 1uih, 1xei, 1xej, 1xek, 2hfm, 2iff, 2lym, 2lyo, 2lyz, 2lzh, 2lzt, 3hfl, 3hfm, 3lym, 3lyo, 3lyt, 3lyz, 3lzt, 4lym, 4lyo, 4lyt, 4lyz, 4lzt, 5lym, 5lyt, 5lyz, 6lyt, 6lyz, 7lyz, 8lyz
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Function

[IVY_ECOLI] Strong inhibitor of lysozyme C. [LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antilysozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such, Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates.

Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria.,Abergel C, Monchois V, Byrne D, Chenivesse S, Lembo F, Lazzaroni JC, Claverie JM Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6394-9. Epub 2007 Apr 3. PMID:17405861^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
↑ Abergel C, Monchois V, Byrne D, Chenivesse S, Lembo F, Lazzaroni JC, Claverie JM. Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria. Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6394-9. Epub 2007 Apr 3. PMID:17405861

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gpq"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gpq RCSB], [http://www.ebi.ac.uk/pdbsum/1gpq PDBsum], [http://www.topsan.org/Proteins/BIGS/1gpq TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/IVY_ECOLI IVY_ECOLI]] Strong inhibitor of lysozyme C. [[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1gpq

From Proteopedia

Revision as of 11:00, 25 December 2014

STRUCTURE OF IVY COMPLEXED WITH ITS TARGET, HEWL

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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