1F89

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

Summary for 1F89

• Entry DOI: 10.2210/pdb1f89/pdb
• Descriptor: 32.5 KDA PROTEIN YLR351C (2 entities in total)
• Functional Keywords: nitrilase, dimer, structural genomics, four layer sandwich, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 65182.43

Authors

Kumaran, D.,Eswaramoorthy, S.,Studier, F.W.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2000-06-29, release date: 2001-10-04, Last modification date: 2024-02-07)

Primary citation

Kumaran, D.,Eswaramoorthy, S.,Gerchman, S.E.,Kycia, H.,Studier, F.W.,Swaminathan, S.
Crystal structure of a putative CN hydrolase from yeast
Proteins, 52:283-291, 2003

PubMed Abstract: 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.

PubMed: 12833551
DOI: 10.1002/prot.10417

Experimental method

X-RAY DIFFRACTION (2.4 Å)