1f89: Difference between revisions

Revision as of 02:51, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f89.png

Template:STRUCTURE 1f89

Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamilyCrystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily

Template:ABSTRACT PUBMED 12833551

About this StructureAbout this Structure

1F89 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a putative CN hydrolase from yeast., Kumaran D, Eswaramoorthy S, Gerchman SE, Kycia H, Studier FW, Swaminathan S, Proteins. 2003 Aug 1;52(2):283-91. PMID:12833551

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OCA

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-'''Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily'''
+===Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily===
-==Overview==
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-The crystal structure of a yeast hypothetical protein with sequence similarity to CN hydrolases has been determined to 2.4 A resolution by the multiwavelength anomalous dispersion (MAD) method. The protein folds as a four-layer alphabetabetaalpha sandwich and exists as a dimer in the crystal and in solution. It was selected in a structural genomics project as representative of CN hydrolases at a time when no structures had been determined for members of this family. Structures for two other members of the family have since been reported and the three proteins have similar topology and dimerization modes, which are distinct from those of other alphabetabetaalpha proteins whose structures are known. The dimers form an unusual eight-layer alphabetabetaalpha:alphabetabetaalpha structure. Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. As with serine hydrolases, the active-site nucleophile (cysteine in this case) is positioned on a nucleophile elbow.
+The line below this paragraph, {{ABSTRACT_PUBMED_12833551}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12833551 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12833551}}
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 [[Category: Psi]]
 [[Category: Structural genomic]]
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