1h09

From Proteopedia

(Difference between revisions)

Current revision

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1

Structural highlights

1h09 is a 1 chain structure with sequence from Streptococcus phage Cp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYS_BPCP1 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. Strictly depends on the presence of choline-containing cell walls for activity.

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

Pneumococcal bacteriophage-encoded lysins are modular choline binding proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) against streptococcal infections. Here we present the crystal structures of the free and choline bound states of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1. While the catalytic module displays an irregular (beta/alpha)(5)beta(3) barrel, the cell wall-anchoring module is formed by six similar choline binding repeats (ChBrs), arranged into two different structural regions: a left-handed superhelical domain configuring two choline binding sites, and a beta sheet domain that contributes in bringing together the whole structure. Crystallographic and site-directed mutagenesis studies allow us to propose a general catalytic mechanism for the whole glycoside hydrolase family 25. Our work provides the first complete structure of a member of the large family of choline binding proteins and reveals that ChBrs are versatile elements able to tune the evolution and specificity of the pneumococcal surface proteins.

Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.,Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M Structure. 2003 Oct;11(10):1239-49. PMID:14527392^[1]

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

References

↑ Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Structure. 2003 Oct;11(10):1239-49. PMID:14527392

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/1h09"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1h09.png|left|200px]]
-<!--
+==Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1==
-The line below this paragraph, containing "STRUCTURE_1h09", creates the "Structure Box" on the page.
+<StructureSection load='1h09' size='340' side='right'caption='[[1h09]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1h09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_phage_Cp1 Streptococcus phage Cp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H09 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=1h09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h09 OCA], [https://pdbe.org/1h09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h09 RCSB], [https://www.ebi.ac.uk/pdbsum/1h09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h09 ProSAT]</span></td></tr>
-{{STRUCTURE_1h09|  PDB=1h09  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LYS_BPCP1 LYS_BPCP1] 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. Strictly depends on the presence of choline-containing cell walls for activity.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/1h09_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h09 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pneumococcal bacteriophage-encoded lysins are modular choline binding proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) against streptococcal infections. Here we present the crystal structures of the free and choline bound states of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1. While the catalytic module displays an irregular (beta/alpha)(5)beta(3) barrel, the cell wall-anchoring module is formed by six similar choline binding repeats (ChBrs), arranged into two different structural regions: a left-handed superhelical domain configuring two choline binding sites, and a beta sheet domain that contributes in bringing together the whole structure. Crystallographic and site-directed mutagenesis studies allow us to propose a general catalytic mechanism for the whole glycoside hydrolase family 25. Our work provides the first complete structure of a member of the large family of choline binding proteins and reveals that ChBrs are versatile elements able to tune the evolution and specificity of the pneumococcal surface proteins.
-===MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1===
+Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.,Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M Structure. 2003 Oct;11(10):1239-49. PMID:14527392<ref>PMID:14527392</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1h09" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14527392}}, adds the Publication Abstract to the page
+*[[Lysin 3D structures|Lysin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14527392 is the PubMed ID number.
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_14527392}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-H09 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_cp-1 Bacteriophage cp-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA].
+[[Category: Large Structures]]
+[[Category: Streptococcus phage Cp1]]
-==Reference==
+[[Category: Albert A]]
-Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1., Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M, Structure. 2003 Oct;11(10):1239-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527392 14527392]
+[[Category: Garcia JL]]
-[[Category: Bacteriophage cp-1]]
+[[Category: Garcia P]]
-[[Category: Lysozyme]]
+[[Category: Hermoso JA]]
-[[Category: Single protein]]
+[[Category: Martinez-Ripoll M]]
-[[Category: Albert, A.]]
+[[Category: Menendez M]]
-[[Category: Garcia, J L.]]
+[[Category: Monterroso B]]
-[[Category: Garcia, P.]]
-[[Category: Hermoso, J A.]]
-[[Category: Martinez-Ripoll, M.]]
-[[Category: Menendez, M.]]
-[[Category: Monterroso, B.]]
-[[Category: Bacteriolytic enzyme]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Lysozyme]]
-[[Category: Multimodular]]
-[[Category: Murein hydrolase]]
-[[Category: Pneumococcal cell wall degradation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:24:26 2008''

1h09

From Proteopedia

Current revision

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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