2fhm

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Current revision (06:40, 1 May 2024) (edit) (undo)
 
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==Solution Structure of Bacillus subtilis Acylphosphatase==
==Solution Structure of Bacillus subtilis Acylphosphatase==
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<StructureSection load='2fhm' size='340' side='right'caption='[[2fhm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2fhm' size='340' side='right'caption='[[2fhm]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2fhm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FHM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2fhm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FHM FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acylphosphatase Acylphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2fhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhm OCA], [https://pdbe.org/2fhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fhm RCSB], [https://www.ebi.ac.uk/pdbsum/2fhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fhm ProSAT], [https://www.topsan.org/Proteins/MCSG/2fhm TOPSAN]</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=2fhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhm OCA], [https://pdbe.org/2fhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fhm RCSB], [https://www.ebi.ac.uk/pdbsum/2fhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fhm ProSAT], [https://www.topsan.org/Proteins/MCSG/2fhm TOPSAN]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACYP_BACSU ACYP_BACSU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2fhm ConSurf].
</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=2fhm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Acylphosphatase is a small enzyme that catalyzes the hydrolysis of acyl phosphates. Here, we present the solution structure of acylphosphatase from Bacillus subtilis (BsAcP), the first from a Gram-positive bacterium. We found that its active site is disordered, whereas it converted to an ordered state upon ligand binding. The structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH (pH&lt;5.8). Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration. This study provides direct evidence for the role of ligand in conformational selection.
 
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Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis.,Hu J, Li D, Su XD, Jin C, Xia B FEBS Lett. 2010 Jul 2;584(13):2852-6. Epub 2010 May 4. PMID:20447399<ref>PMID:20447399</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2fhm" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
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[[Category: Acylphosphatase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hu, J C]]
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[[Category: Hu JC]]
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[[Category: Xia, B]]
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[[Category: Xia B]]
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[[Category: Hydrolase]]
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Current revision

Solution Structure of Bacillus subtilis Acylphosphatase

PDB ID 2fhm

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