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| | ==E185A mutant of peptidoglycan hydrolase from Sphingomonas sp. A1== | | ==E185A mutant of peptidoglycan hydrolase from Sphingomonas sp. A1== |
| - | <StructureSection load='3k3t' size='340' side='right' caption='[[3k3t]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3k3t' size='340' side='right'caption='[[3k3t]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k3t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp._a1 Sphingomonas sp. a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K3T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._A1 Sphingomonas sp. A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K3T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zyc|2zyc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flgJ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90322 Sphingomonas sp. A1])</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=3k3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k3t OCA], [https://pdbe.org/3k3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k3t RCSB], [https://www.ebi.ac.uk/pdbsum/3k3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k3t 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=3k3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k3t OCA], [http://pdbe.org/3k3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k3t RCSB], [http://www.ebi.ac.uk/pdbsum/3k3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k3t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B7XH69_9SPHN B7XH69_9SPHN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sphingomonas sp. a1]] | + | [[Category: Large Structures]] |
| - | [[Category: Hashimoto, W]] | + | [[Category: Sphingomonas sp. A1]] |
| - | [[Category: Itoh, T]] | + | [[Category: Hashimoto W]] |
| - | [[Category: Maruyama, Y]] | + | [[Category: Itoh T]] |
| - | [[Category: Mikami, B]] | + | [[Category: Maruyama Y]] |
| - | [[Category: Murata, K]] | + | [[Category: Mikami B]] |
| - | [[Category: Ochiai, A]] | + | [[Category: Murata K]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Ochiai A]] |
| Structural highlights
Function
B7XH69_9SPHN
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
The flagellar protein FlgJ, a member of glycoside hydrolase family 73, has N- and C-terminal domains that are responsible for flagellar rod assembly and peptidoglycan hydrolysis, respectively. The crystal structure of the C-terminal domain of SPH1045 (SPH1045-C), the FlgJ from Sphingomonas sp. strain A1, showed a long cleft formed by two lobes, alpha and beta. In this study, seven site-specific mutants of residues in the cleft were prepared and analyzed. Enzyme activity was reduced most significantly in mutants E185A and Y281A, followed by E224A. A comparison of the crystal structure of the inactive mutant E185A with that of other related enzymes revealed that Glu185 is structurally reasonable as the proton donor and that Tyr281 is close to Glu185. Glu224 is, however, far from the catalytic site, which is inconsistent with the decreased activity exhibited by E224A. The structural flexibility of Glu224 and its neighboring residues observed in SPH1045-C may indicate that this region is able to change its conformation upon substrate binding. ((c) 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim).
Mutational studies of the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1.,Maruyama Y, Ochiai A, Itoh T, Mikami B, Hashimoto W, Murata K J Basic Microbiol. 2010 Jun 28. PMID:20586063[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maruyama Y, Ochiai A, Itoh T, Mikami B, Hashimoto W, Murata K. Mutational studies of the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1. J Basic Microbiol. 2010 Jun 28. PMID:20586063 doi:10.1002/jobm.200900249
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