1xju

From Proteopedia

(Difference between revisions)

Revision as of 13:15, 12 October 2017

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

Structural highlights

1xju is a 2 chain structure with sequence from Bpp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	17, LYSA, LyZ (BPP1)
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYS_BPP1] Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity (By similarity).

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

The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.

Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.,Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, Young R Science. 2005 Jan 7;307(5706):113-7. PMID:15637279^[1]

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

References

↑ Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, Young R. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science. 2005 Jan 7;307(5706):113-7. PMID:15637279 doi:307/5706/113

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/1xju"

@@ Line 1: / Line 1: @@
 ==Crystal structure of secreted inactive form of P1 phage endolysin Lyz==
 <StructureSection load='1xju' size='340' side='right' caption='[[1xju]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">17, LYSA, LyZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10678 BPP1])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
-<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=1xju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xju OCA], [http://pdbe.org/1xju PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xju RCSB], [http://www.ebi.ac.uk/pdbsum/1xju PDBsum]</span></td></tr>
+<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=1xju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xju OCA], [http://pdbe.org/1xju PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xju RCSB], [http://www.ebi.ac.uk/pdbsum/1xju PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xju ProSAT]</span></td></tr>
 </table>
 == Function ==

1xju

From Proteopedia

Revision as of 13:15, 12 October 2017

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

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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