1f89: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F89 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1f89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F89 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f89 RCSB], [http://www.ebi.ac.uk/pdbsum/1f89 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1f89 TOPSAN]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f89 RCSB], [http://www.ebi.ac.uk/pdbsum/1f89 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1f89 TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Burley, S K | [[Category: Burley, S K]] | ||
[[Category: Eswaramoorthy, S | [[Category: Eswaramoorthy, S]] | ||
[[Category: Kumaran, D | [[Category: Kumaran, D]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Studier, F W | [[Category: Studier, F W]] | ||
[[Category: Swaminathan, S | [[Category: Swaminathan, S]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
[[Category: Four layer sandwich]] | [[Category: Four layer sandwich]] | ||
[[Category: Nitrilase]] | [[Category: Nitrilase]] | ||
[[Category: | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]] | ||
[[Category: Protein structure initiative | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 15:45, 6 November 2014
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
Structural highlights
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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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