1v73: Difference between revisions

Revision as of 12:13, 28 July 2008

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File:1v73.png

Template:STRUCTURE 1v73

Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.

Template:ABSTRACT PUBMED 15713885

About this StructureAbout this Structure

1V73 is a Single protein structure of sequence from Shewanella sp.. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp., Tsuruta H, Mikami B, Aizono Y, J Biochem. 2005 Jan;137(1):69-77. PMID:15713885

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-'''Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.'''
+===Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.===
-==Overview==
+<!--
-The cold-active protein-tyrosine phosphatase (CAPTPase) of a psychrophile, Shewanella sp., shows high catalytic activity below 20 degrees C. The catalytic residue of CAPTPase is histidine, as opposed to the cysteine of known protein-tyrosine phosphatases (PTPases), and the enzyme protein has three amino acid sequences, Asp-Xaa-His, Gly-Asp-Xaa-Xaa-Asp-Arg and Gly-Asn-His-Glu, that are observed in many protein-serine/threonine phosphatases (PS/TPases). We have determined the crystal structures of CAPTPase at 1.82 angstroms and the enzyme bound with a phosphate ion at 1.90 angstroms resolution using X-ray crystallography and the multiple isomorphous replacement method. The final refined models are comprised of 331 amino acid residues, two metal ions, 447 water molecules, and an acetate or phosphate ion in an asymmetric unit. The enzyme protein consists of three beta-sheets, termed Sheet I, Sheet I', and Sheet II, and 14 alpha-helices. The CAPTPase has a different overall structure from known protein-tyrosine phosphatases. The arrangement of two metal ions, a phosphate ion and the adjacent amino acid residues in the catalytic site of CAPTPase is identical to that of PS/TPases. Thus, it was confirmed that the CAPTPase was a novel PTPase with a conformation similar to the catalytic site of PS/TPase. We speculate that the hydrophobic moiety around the catalytic residue of CAPTPase might play an important role in eliciting high activity at low temperature.
+The line below this paragraph, {{ABSTRACT_PUBMED_15713885}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15713885 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15713885}}
 ==About this Structure==
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 [[Category: Psychrophile]]
 [[Category: Shewanella sp]]
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