1yny

From Proteopedia

(Difference between revisions)

Current revision

Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition

Structural highlights

1yny is a 2 chain structure with sequence from Bacillus sp. AR9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5DLU2_9BACI

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Radha Kishan KV, Vohra RM, Ganesan K, Agrawal V, Sharma VM, Sharma R. Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition. J Mol Biol. 2005 Mar 18;347(1):95-105. Epub 2005 Jan 27. PMID:15733920 doi:10.1016/j.jmb.2005.01.025

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yny"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yny' size='340' side='right'caption='[[1yny]], [[Resolution|resolution]] 2.30&Aring;' 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>
+<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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] </span></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]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus sp. ar9]]
+[[Category: Bacillus sp. AR9]]
-[[Category: Dihydropyrimidinase]]
 [[Category: Large Structures]]
-[[Category: Agrawal, V]]
+[[Category: Agrawal V]]
-[[Category: Ganeshan, K]]
+[[Category: Ganeshan K]]
-[[Category: Kishan, K V.Radha]]
+[[Category: Radha Kishan KV]]
-[[Category: Sharma, R]]
+[[Category: Sharma R]]
-[[Category: Sharma, V M]]
+[[Category: Sharma VM]]
-[[Category: Vohra, R M]]
+[[Category: Vohra RM]]
-[[Category: Binuclear metal-binding]]
-[[Category: Hydantoinase]]
-[[Category: Hydrolase]]
-[[Category: Tim-barrel]]

1yny

From Proteopedia

Current revision

Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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