1yny
From Proteopedia
(Difference between revisions)
| (11 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1yny.gif|left|200px]] | ||
| - | + | ==Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition== | |
| - | + | <StructureSection load='1yny' size='340' side='right'caption='[[1yny]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1yny]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._AR9 Bacillus sp. AR9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YNY 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]] 2.3Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1yny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yny OCA], [https://pdbe.org/1yny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yny RCSB], [https://www.ebi.ac.uk/pdbsum/1yny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yny ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q5DLU2_9BACI Q5DLU2_9BACI] | |
| - | + | == 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/yn/1yny_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1yny ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Stereospecific conversion of hydantoins into their carbamoyl acid derivatives could be achieved by using the enzyme hydantoinase. Specific hydantoinases convert either the D-form or the L-form of the hydantoin and the amino acids responsible for stereospecificity have not been identified. Structural studies on hydantoinases from a few bacterial species were published recently. The structure of a thermostable D-hydantoinase from Bacillus sp. AR9 (bar9HYD) was solved to 2.3 angstroms resolution. The usual modification of carboxylation of the active-site residue Lys150 did not happen in bar9HYD. Two manganese ions were modelled in the active site. Through biochemical studies, it was shown that mercury inhibits the activity of the enzyme. The mercury derivative provided some information about the binding site of the mercuric inhibitors and a possible reason for inhibition is presented. | Stereospecific conversion of hydantoins into their carbamoyl acid derivatives could be achieved by using the enzyme hydantoinase. Specific hydantoinases convert either the D-form or the L-form of the hydantoin and the amino acids responsible for stereospecificity have not been identified. Structural studies on hydantoinases from a few bacterial species were published recently. The structure of a thermostable D-hydantoinase from Bacillus sp. AR9 (bar9HYD) was solved to 2.3 angstroms resolution. The usual modification of carboxylation of the active-site residue Lys150 did not happen in bar9HYD. Two manganese ions were modelled in the active site. Through biochemical studies, it was shown that mercury inhibits the activity of the enzyme. The mercury derivative provided some information about the binding site of the mercuric inhibitors and a possible reason for inhibition is presented. | ||
| - | + | Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition.,Radha Kishan KV, Vohra RM, Ganesan K, Agrawal V, Sharma VM, Sharma R J Mol Biol. 2005 Mar 18;347(1):95-105. Epub 2005 Jan 27. PMID:15733920<ref>PMID:15733920</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1yny" style="background-color:#fffaf0;"></div> |
| - | [[Category: Agrawal | + | == References == |
| - | [[Category: Ganeshan | + | <references/> |
| - | [[Category: Kishan | + | __TOC__ |
| - | [[Category: Sharma | + | </StructureSection> |
| - | [[Category: Sharma | + | [[Category: Bacillus sp. AR9]] |
| - | [[Category: Vohra | + | [[Category: Large Structures]] |
| - | + | [[Category: Agrawal V]] | |
| - | + | [[Category: Ganeshan K]] | |
| - | + | [[Category: Radha Kishan KV]] | |
| - | + | [[Category: Sharma R]] | |
| - | + | [[Category: Sharma VM]] | |
| + | [[Category: Vohra RM]] | ||
Current revision
Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition
| |||||||||||
