2ex6
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2ex6.png|left|200px]] | ||
- | < | + | ==Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin== |
- | + | <StructureSection load='2ex6' size='340' side='right'caption='[[2ex6]], [[Resolution|resolution]] 1.60Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2ex6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EX6 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIX:(2R,4S)-2-[(1R)-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>AIX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2ex6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ex6 OCA], [https://pdbe.org/2ex6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ex6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ex6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ex6 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DACB_ECOLI DACB_ECOLI] Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction.<ref>PMID:2046551</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/ex/2ex6_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ex6 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in the synthesis and maintenance of the cell wall. The model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds. The structures of the protein covalently attached to five different antibiotics presented here show the active site residues are unmoved compared to the apoprotein, but nearby surface loops and helices are displaced in some cases. The altered geometry of conserved active site residues compared with those of other PBPs suggests a possible cause for the slow deacylation rate of PBP4. | ||
- | + | Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics.,Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754<ref>PMID:16411754</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2ex6" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Penicillin-binding protein|Penicillin-binding protein]] | |
- | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
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- | == | + | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Kishida | + | [[Category: Large Structures]] |
- | [[Category: Lloyd | + | [[Category: Kishida H]] |
- | [[Category: Park | + | [[Category: Lloyd A]] |
- | [[Category: Roper | + | [[Category: Park S-Y]] |
- | [[Category: Tame | + | [[Category: Roper DI]] |
- | [[Category: Unzai | + | [[Category: Tame JRH]] |
- | + | [[Category: Unzai S]] | |
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Current revision
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin
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Categories: Escherichia coli | Large Structures | Kishida H | Lloyd A | Park S-Y | Roper DI | Tame JRH | Unzai S