Crystal structure of VC0702 at 2.0 Å:: Conserved hypothetical protein from Vibrio cholerae

被引:2
作者
Ni, Shuisong
Forouhar, Farhad
Bussiere, Dirksen E.
Robinson, Howard
Kennedy, Michael A.
机构
[1] Pacific NW Natl Lab, Div Biol Sci, Richland, WA 99352 USA
[2] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA
[3] Chiron Corp, Emeryville, CA 94608 USA
[4] Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA
关键词
Vibrio cholerae; VC0702; biofilm regulation; dNTPase; pyrophosphatase; VC0703; MbaA; dUTPase;
D O I
10.1002/prot.20919
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
VC0702, a conserved hypothetical protein of unknown function from Vibrio cholerae, resides in a three-gene operon containing the MbaA gene that encodes for a GGDEF and EAL domain-containing protein which is involved in regulating formation of the extracellular matrix of biofilms in Vibrio cholerae. The VC0702 crystal structure has been determined at 2.0 angstrom and refined to R-work = 22.8% and R-free = 26.3%. VC0702 crystallized in an orthorhombic crystal lattice in the C222(1) space group with dimensions of a = 66.61 angstrom, b = 88.118 angstrom, and c = 118.35 angstrom with a homodimer in the asymmetric unit. VC0702, which forms a mixed alpha + beta three-layered alpha beta alpha sandwich, belongs to the Pfam DUF84 and COG1986 families of proteins. Sequence conservation within the DUF84 and COG1986 families was used to identify a conserved patch of surface residues that define a cleft and potential substrate-binding site in VC0702. The three-dimensional structure of VC0702 is similar to that of Mj0226 from Methanococcus janeschii, which has been identified as a novel NTPase that binds NTP in a deep cleft similarly located to the conserved patch of surface residues that define an analogous cleft in VC0702. Collectively, the data suggest that VC0702 may have a biochemical function that involves NTP binding and phosphatase activity of some kind, and is likely involved in regulation of the signaling pathway that controls biofilm formation and maintenance in Vibrio cholerae.
引用
收藏
页码:733 / 741
页数:9
相关论文
共 16 条
[11]   Reciprocal-space solvent flattening [J].
Terwilliger, TC .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1999, 55 :1863-1871
[12]   Maximum-likelihood density modification using pattern recognition of structural motifs [J].
Terwilliger, TC .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 :1755-1762
[13]   Automated MAD and MIR structure solution [J].
Terwilliger, TC ;
Berendzen, J .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1999, 55 :849-861
[14]   Maximum-likelihood density modification [J].
Terwilliger, TC .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 :965-972
[15]   Map-likelihood phasing [J].
Terwilliger, TC .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2001, 57 :1763-1775
[16]   CLUSTAL-W - IMPROVING THE SENSITIVITY OF PROGRESSIVE MULTIPLE SEQUENCE ALIGNMENT THROUGH SEQUENCE WEIGHTING, POSITION-SPECIFIC GAP PENALTIES AND WEIGHT MATRIX CHOICE [J].
THOMPSON, JD ;
HIGGINS, DG ;
GIBSON, TJ .
NUCLEIC ACIDS RESEARCH, 1994, 22 (22) :4673-4680