| Crystallization and preliminary diffraction studies of Nudix hydrolase YmfB from Escherichia coli K-1. | |
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MedLine Citation:
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PMID: 19149682 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Nudix hydrolases are a family of proteins that contains the Nudix signature of the characteristic amino-acid sequence Gx(5)Ex(5) [UA]xREx(2)EExGU, where x represents any amino acid and U usually a bulky hydrophobic amino acid, such as Leu, Val, or Ile. They ubiquitously exist in more than 200 species. YmfB, a novel Nudix hydrolase found in Escherichia coli, is a nonspecific nucleoside tri- and di-phosphatase, which atypically releases inorganic orthophosphate from triphosphates instead of pyrophosphate. In this study, YmfB was cloned, overexpressed, and crystallized. Two different crystals, one belonging to an orthorhombic space group C222(1) and the other a monoclinic space group P2(1), diffracted to 2.7 A and 2.6 A resolution, and had unit cell parameters of a = 68.7 A, b = 283.1 A, c = 70.4 A and a = 69.1 A, b = 70.3 A, c = 145.6 A, beta = 103.3 degrees , respectively. For the C222(1) space group, four or five monomers exist in the asymmetric unit, with a corresponding V(m) of 2.48 or 1.99 A(3) Da(-1) and a solvent content of 50.5 or 38.2%. For the P2(1) space group, eight or nine monomers exist in the asymmetric unit, with a corresponding V(m) of 2.49 or 2.21 A(3) Da(-1) and a solvent content of 50.7 or 44.5%. |
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Authors:
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Myoung-Ki Hong; Jin-Kwang Kim; Yeh-Jin Ahn; Lin-Woo Kang |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Protein and peptide letters Volume: 16 ISSN: 0929-8665 ISO Abbreviation: Protein Pept. Lett. Publication Date: 2009 |
Date Detail:
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Created Date: 2009-01-19 Completed Date: 2009-03-05 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9441434 Medline TA: Protein Pept Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 101-4 Citation Subset: IM |
Affiliation:
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Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Cloning, Molecular Crystallization Crystallography, X-Ray Escherichia coli / enzymology* Escherichia coli Proteins / chemistry* Pyrophosphatases / chemistry* Sequence Alignment |
| Chemical | |
Reg. No./Substance:
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0/Escherichia coli Proteins; EC 3.6.1.-/Pyrophosphatases; EC 3.6.1.-/YmfB protein, E coli |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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