1ta1: Difference between revisions
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[[Image:1ta1.gif|left|200px]] | [[Image:1ta1.gif|left|200px]] | ||
'''H141C mutant of rat liver arginase I''' | {{Structure | ||
|PDB= 1ta1 |SIZE=350|CAPTION= <scene name='initialview01'>1ta1</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] | |||
|GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |||
}} | |||
'''H141C mutant of rat liver arginase I''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TA1 is a [ | 1TA1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TA1 OCA]. | ||
==Reference== | ==Reference== | ||
Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:[http:// | Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16266687 16266687] | ||
[[Category: Arginase]] | [[Category: Arginase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: h141c mutation]] | [[Category: h141c mutation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:15:50 2008'' | ||
Revision as of 15:15, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ARG1 (Rattus norvegicus) | ||||||
| Activity: | Arginase, with EC number 3.5.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
H141C mutant of rat liver arginase I
OverviewOverview
Rat liver arginase (arginase I) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the inactivation process at pH 7.0, 25 degrees C. Partial protection from inactivation is provided by the product of the reaction, l-ornithine, while nearly complete protection is afforded by the inhibitor pair, l-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141 towards diethyl pyrocarbonate can be explained by its proximity to E277. A proton shuttling role for H141 is supported by its conformational mobility observed among the known arginase structures. H141 is proposed to serve as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure.
About this StructureAbout this Structure
1TA1 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:16266687
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