1oba

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:33, 13 December 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1oba.gif|left|200px]]
 
-
{{Structure
+
==Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1 complexed with choline==
-
|PDB= 1oba |SIZE=350|CAPTION= <scene name='initialview01'>1oba</scene>, resolution 2.45&Aring;
+
<StructureSection load='1oba' size='340' side='right'caption='[[1oba]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=CH1:Cht+Binding+Site+For+Chain+A'>CH1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>
+
<table><tr><td colspan='2'>[[1oba]] 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=1OBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OBA FirstGlance]. <br>
-
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oba OCA], [https://pdbe.org/1oba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oba RCSB], [https://www.ebi.ac.uk/pdbsum/1oba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oba ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oba OCA], [http://www.ebi.ac.uk/pdbsum/1oba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oba RCSB]</span>
+
== 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 ==
-
'''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1 COMPLEXED WITH CHOLINE'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ob/1oba_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=1oba 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.
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.
-
==About this Structure==
+
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>
-
1OBA 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=1OBA OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Bacteriophage cp-1]]
+
<div class="pdbe-citations 1oba" style="background-color:#fffaf0;"></div>
-
[[Category: Lysozyme]]
+
-
[[Category: Single protein]]
+
-
[[Category: Albert, A.]]
+
-
[[Category: Garcia, J L.]]
+
-
[[Category: Garcia, P.]]
+
-
[[Category: Hermoso, J A.]]
+
-
[[Category: Martinez-Ripoll, M.]]
+
-
[[Category: Menendez, M.]]
+
-
[[Category: Monterroso, B.]]
+
-
[[Category: choline]]
+
-
[[Category: lysozyme]]
+
-
[[Category: multimodular]]
+
-
[[Category: murein hydrolase]]
+
-
[[Category: phage cp-1 lysin]]
+
-
[[Category: pneumococcal cell wall degradation,hydrolase glycosidase,bacterilytic enzyme]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:40 2008''
+
==See Also==
 +
*[[Lysin 3D structures|Lysin 3D structures]]
 +
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Streptococcus phage Cp1]]
 +
[[Category: Albert A]]
 +
[[Category: Garcia JL]]
 +
[[Category: Garcia P]]
 +
[[Category: Hermoso JA]]
 +
[[Category: Martinez-Ripoll M]]
 +
[[Category: Menendez M]]
 +
[[Category: Monterroso B]]

Current revision

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1 complexed with choline

PDB ID 1oba

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oba"
Personal tools