1aps
From Proteopedia
(Difference between revisions)
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==THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS== | ==THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS== | ||
| - | <StructureSection load='1aps' size='340' side='right'caption='[[1aps | + | <StructureSection load='1aps' size='340' side='right'caption='[[1aps]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APS FirstGlance]. <br> | <table><tr><td colspan='2'>[[1aps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APS FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </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=1aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aps OCA], [https://pdbe.org/1aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aps RCSB], [https://www.ebi.ac.uk/pdbsum/1aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aps ProSAT]</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=1aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aps OCA], [https://pdbe.org/1aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aps RCSB], [https://www.ebi.ac.uk/pdbsum/1aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aps ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ACYP2_HORSE ACYP2_HORSE] Its physiological role is not yet clear. | |
== 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=1aps 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=1aps ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We report here the complete determination of the solution structure of acylphosphatase, a small enzyme that catalyses the hydrolysis of organic acylphosphates, as determined by distance geometry methods based on nuclear magnetic resonance information. A non-standard strategy for the distance geometry calculations was used and is described here some detail. The five best structures were then refined by restrained energy minimization and molecular dynamics in order to explore the conformational space consistent with the experimental data. We address the question of whether the solution structure of acylphosphatase follows the general principles of protein structure, i.e. those learned from analysing crystal structures. Static and dynamic features are discussed in detail. An uncommon beta-alpha-beta motif, so far found only in procarboxypeptidase B and in an RNA-binding protein, is present in acylphosphatase. | ||
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| - | Three-dimensional structure of acylphosphatase. Refinement and structure analysis.,Pastore A, Saudek V, Ramponi G, Williams RJ J Mol Biol. 1992 Mar 20;224(2):427-40. PMID:1313885<ref>PMID:1313885</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1aps" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Acylphosphatase]] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Pastore | + | [[Category: Pastore A]] |
| - | [[Category: Ramponi | + | [[Category: Ramponi G]] |
| - | [[Category: Saudek | + | [[Category: Saudek V]] |
| - | [[Category: Williams | + | [[Category: Williams RJP]] |
Revision as of 15:27, 13 March 2024
THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS
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