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5i8l

From Proteopedia

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Current revision

Crystal structure of the full-length cell wall-binding module of Cpl7 mutant R223A

Structural highlights

5i8l is a 1 chain structure with sequence from Streptococcus phage CP-7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.801Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYS_BPCP7 Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Degrades cell walls containing either choline or ethanolamine.

Publication Abstract from PubMed

Endolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW_7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW_7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-acetyl-D-glucosaminyl-(beta1,4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) as the peptidoglycan (PG) target recognized by the CW_7 motifs, and characterize feasible GMDP-CW_7 contacts. Our data suggest that Cpl-7 cell wall-binding domain might simultaneously bind to three PG chains, and also highlight the potential use of CW_7-containing lysins as novel anti-infectives.

Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.,Bustamante N, Iglesias-Bexiga M, Bernardo-Garcia N, Silva-Martin N, Garcia G, Campanero-Rhodes MA, Garcia E, Uson I, Buey RM, Garcia P, Hermoso JA, Bruix M, Menendez M Sci Rep. 2017 Nov 28;7(1):16494. doi: 10.1038/s41598-017-16392-4. PMID:29184076^[1]

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

References

↑ Bustamante N, Iglesias-Bexiga M, Bernardo-Garcia N, Silva-Martin N, Garcia G, Campanero-Rhodes MA, Garcia E, Uson I, Buey RM, Garcia P, Hermoso JA, Bruix M, Menendez M. Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan. Sci Rep. 2017 Nov 28;7(1):16494. doi: 10.1038/s41598-017-16392-4. PMID:29184076 doi:http://dx.doi.org/10.1038/s41598-017-16392-4

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5i8l"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the full-length cell wall-binding module of Cpl7 mutant R223A==
-<StructureSection load='5i8l' size='340' side='right' caption='[[5i8l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='5i8l' size='340' side='right'caption='[[5i8l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5i8l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpcp7 Bpcp7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I8L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5i8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_phage_CP-7 Streptococcus phage CP-7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I8L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.801&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPL7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10748 BPCP7])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5i8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8l OCA], [https://pdbe.org/5i8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i8l RCSB], [https://www.ebi.ac.uk/pdbsum/5i8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8l ProSAT]</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=5i8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8l OCA], [http://pdbe.org/5i8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i8l RCSB], [http://www.ebi.ac.uk/pdbsum/5i8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LYS_BPCP7 LYS_BPCP7]] Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Degrades cell walls containing either choline or ethanolamine.
+[https://www.uniprot.org/uniprot/LYS_BPCP7 LYS_BPCP7] Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Degrades cell walls containing either choline or ethanolamine.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Bpcp7]]
+[[Category: Large Structures]]
-[[Category: Lysozyme]]
+[[Category: Streptococcus phage CP-7]]
-[[Category: Bernardo-Garcia, N]]
+[[Category: Bernardo-Garcia N]]
-[[Category: Hermoso, J A]]
+[[Category: Hermoso JA]]
-[[Category: Silva-Martin, N]]
+[[Category: Silva-Martin N]]
-[[Category: Uson, I]]
+[[Category: Uson I]]
-[[Category: Cell-wall binding domain]]
-[[Category: Hydrolase]]

5i8l

From Proteopedia

Current revision

Crystal structure of the full-length cell wall-binding module of Cpl7 mutant R223A

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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