1yny
From Proteopedia
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|PDB= 1yny |SIZE=350|CAPTION= <scene name='initialview01'>1yny</scene>, resolution 2.30Å | |PDB= 1yny |SIZE=350|CAPTION= <scene name='initialview01'>1yny</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yny OCA], [http://www.ebi.ac.uk/pdbsum/1yny PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yny RCSB]</span> | ||
}} | }} | ||
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[[Category: Sharma, V M.]] | [[Category: Sharma, V M.]] | ||
[[Category: Vohra, R M.]] | [[Category: Vohra, R M.]] | ||
| - | [[Category: | + | [[Category: binuclear metal-binding]] |
| - | [[Category: tim-barrel | + | [[Category: hydantoinase]] |
| + | [[Category: hydrolase]] | ||
| + | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:14:59 2008'' |
Revision as of 22:15, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Dihydropyrimidinase, with EC number 3.5.2.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition
Overview
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.
About this Structure
1YNY is a Protein complex structure of sequences from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
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
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