1ocy

From Proteopedia

(Difference between revisions)

Current revision

Structure of the receptor-binding domain of the bacteriophage T4 short tail fibre

Structural highlights

1ocy is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FIB12_BPT4 Structural component of the short tail fiber. Adhesion protein that binds irreversibly to the lipopolysaccharides component (LPS) on the cell surface of Escherichia coli B strains during virus attachment. After at least three long tail fibers have bound, short tail fibers extend and bind irreversibly to the core region of the host cell LPS.^[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

Adsorption of T4 bacteriophage to the Escherichia coli host cell is mediated by six long and six short tail fibres. After at least three long tail fibres have bound, short tail fibres extend and bind irreversibly to the core region of the host cell lipo-polysaccharide (LPS), serving as inextensible stays during penetration of the cell envelope by the tail tube. The short tail fibres consist of a parallel, in-register, trimer of gene product 12 (gp12).X-ray crystallography at 1.5A resolution of a protease-stable fragment of gp12 generated in the presence of zinc chloride reveals the structure of the C-terminal receptor-binding domain. It has a novel "knitted" fold, consisting of three extensively intertwined monomers. It reveals a metal-binding site, containing a zinc ion coordinated by six histidine residues in an octahedral conformation. We also suggest an LPS-binding region.

The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold.,Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, Miller S, van Raaij MJ J Mol Biol. 2003 Aug 8;331(2):361-73. PMID:12888344^[2]

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

References

↑ Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. PMID:12837775
↑ Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, Miller S, van Raaij MJ. The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J Mol Biol. 2003 Aug 8;331(2):361-73. PMID:12888344

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-==STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF THE BACTERIOPHAGE T4 SHORT TAIL FIBRE==
-<StructureSection load='1ocy' size='340' side='right' caption='[[1ocy]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+==Structure of the receptor-binding domain of the bacteriophage T4 short tail fibre==
+<StructureSection load='1ocy' size='340' side='right'caption='[[1ocy]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ocy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OCY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ocy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OCY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h6w|1h6w]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1ocy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocy OCA], [http://pdbe.org/1ocy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ocy RCSB], [http://www.ebi.ac.uk/pdbsum/1ocy PDBsum]</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=1ocy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocy OCA], [https://pdbe.org/1ocy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ocy RCSB], [https://www.ebi.ac.uk/pdbsum/1ocy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ocy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VG12_BPT4 VG12_BPT4]] Structural component of the short tail fiber. Secondary adhesin that binds irreversibly to the lipopolysaccharides component on the cell surface of Escherichia coli B strains during virus attachment.
+[https://www.uniprot.org/uniprot/FIB12_BPT4 FIB12_BPT4] Structural component of the short tail fiber. Adhesion protein that binds irreversibly to the lipopolysaccharides component (LPS) on the cell surface of Escherichia coli B strains during virus attachment. After at least three long tail fibers have bound, short tail fibers extend and bind irreversibly to the core region of the host cell LPS.<ref>PMID:12837775</ref>
 == 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/oc/1ocy_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1ocy_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bpt4]]
+[[Category: Escherichia virus T4]]
-[[Category: Gielen, G]]
+[[Category: Large Structures]]
-[[Category: Miller, S]]
+[[Category: Gielen G]]
-[[Category: Raaij, M J.Van]]
+[[Category: Miller S]]
-[[Category: Schuetz, M]]
+[[Category: Schuetz M]]
-[[Category: Thomassen, E]]
+[[Category: Thomassen E]]
-[[Category: Bacteriophage structural protein]]
+[[Category: Van Raaij MJ]]
-[[Category: Baseplate protein]]
-[[Category: Fibrous protein]]
-[[Category: Gene product 12]]
-[[Category: Lipo-polysaccharide binding]]
-[[Category: Structural protein]]

1ocy

From Proteopedia

Current revision

Structure of the receptor-binding domain of the bacteriophage T4 short tail fibre

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox