Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

被引：10
|
作者：
Xu, Qingping [1 ,2 ]
Grant, Joanna [1 ,3 ]
Chiu, Hsiu-Ju [1 ,2 ]
Farr, Carol L. [1 ,4 ]
Jaroszewski, Lukasz [1 ,5 ,6 ]
Knuth, Mark W. [1 ,3 ]
Miller, Mitchell D. [1 ,2 ]
Lesley, Scott A. [1 ,3 ,4 ]
Godzik, Adam [1 ,5 ,6 ]
Elsliger, Marc-Andre [1 ,4 ]
Deacon, Ashley M. [1 ,2 ]
Wilson, Ian A. [1 ,4 ]
机构：
[1] Joint Ctr Struct Genom, La Jolla, CA USA
[2] SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA 94025 USA
[3] Novartis Res Fdn, Genom Inst, Prot Sci Dept, San Diego, CA 92121 USA
[4] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA
[5] Univ Calif San Diego, Ctr Res Biol Syst, La Jolla, CA 92093 USA
[6] Sanford Burnham Med Res Inst, Program Bioinformat & Syst Biol, La Jolla, CA 92037 USA
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2014年 / 82卷 / 01期
关键词：
PF10014; BsmA; cupin dioxygenase; free amino acids; 2-oxyglutarate; ferrous iron; BIOSYNTHETIC GENE-CLUSTER; SERVER;
D O I：
10.1002/prot.24362
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：
PF10014 is a novel family of 2-oxyglutarate-Fe2+-dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 angstrom resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the -strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site. Proteins 2014; 82:164-170. (c) 2013 Wiley Periodicals, Inc.
引用
收藏
页码：164 / 170
页数：7
相关论文
共 26 条
  • [21] The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold
    Cooper, SJ
    Leonard, GA
    McSweeney, SM
    Thompson, AW
    Naismith, JH
    Qamar, S
    Plater, A
    Berry, A
    Hunter, WN
    STRUCTURE, 1996, 4 (11) : 1303 - 1315
  • [22] Crystal Structure of the Cystic Fibrosis Transmembrane Conductance Regulator Inhibitory Factor Cif Reveals Novel Active-Site Features of an Epoxide Hydrolase Virulence Factor
    Bahl, Christopher D.
    Morisseau, Christophe
    Bomberger, Jennifer M.
    Stanton, Bruce A.
    Hammock, Bruce D.
    O'Toole, George A.
    Madden, Dean R.
    JOURNAL OF BACTERIOLOGY, 2010, 192 (07) : 1785 - 1795
  • [23] Crystal structure of Streptococcus pneumoniae N-acetyl-glucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
    Sulzenbacher, G
    Gal, L
    Peneff, C
    Fassy, F
    Bourne, Y
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (15) : 11844 - 11851
  • [24] Crystal structure of a multidrug-resistant HIV-1 protease clinical isolate reveals an expanded active site cavity and represents a novel target for the design of protease inhibitors
    Kovari, LC
    Vickrey, JF
    Logsdon, BC
    Proteasa, G
    Wawrzak, Z
    Winters, MA
    Merigan, TC
    ANTIVIRAL THERAPY, 2003, 8 (03) : U53 - U53
  • [25] The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role
    Krishna, S. Sri
    Aravind, L.
    Bakolitsa, Constantina
    Caruthers, Jonathan
    Carlton, Dennis
    Miller, Mitchell D.
    Abdubek, Polat
    Astakhova, Tamara
    Axelrod, Herbert L.
    Chiu, Hsiu-Ju
    Clayton, Thomas
    Deller, Marc C.
    Duan, Lian
    Feuerhelm, Julie
    Grant, Joanna C.
    Han, Gye Won
    Jaroszewski, Lukasz
    Jin, Kevin K.
    Klock, Heath E.
    Knuth, Mark W.
    Kumar, Abhinav
    Marciano, David
    McMullan, Daniel
    Morse, Andrew T.
    Nigoghossian, Edward
    Okach, Linda
    Reyes, Ron
    Rife, Christopher L.
    van den Bedem, Henry
    Weekes, Dana
    Xu, Qingping
    Hodgson, Keith O.
    Wooley, John
    Elsliger, Marc-Andre
    Deacon, Ashley M.
    Godzik, Adam
    Lesley, Scott A.
    Wilson, Ian A.
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2010, 66 : 1160 - 1166
  • [26] Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation
    Miller, Mitchell D.
    Aravind, L.
    Bakolitsa, Constantina
    Rife, Christopher L.
    Carlton, Dennis
    Abdubek, Polat
    Astakhova, Tamara
    Axelrod, Herbert L.
    Chiu, Hsiu-Ju
    Clayton, Thomas
    Deller, Marc C.
    Duan, Lian
    Feuerhelm, Julie
    Grant, Joanna C.
    Han, Gye Won
    Jaroszewski, Lukasz
    Jin, Kevin K.
    Klock, Heath E.
    Knuth, Mark W.
    Kozbial, Piotr
    Krishna, S. Sri
    Kumar, Abhinav
    Marciano, David
    McMullan, Daniel
    Morse, Andrew T.
    Nigoghossian, Edward
    Okach, Linda
    Reyes, Ron
    van den Bedem, Henry
    Weekes, Dana
    Xu, Qingping
    Hodgson, Keith O.
    Wooley, John
    Elsliger, Marc-Andre
    Deacon, Ashley M.
    Godzik, Adam
    Lesley, Scott A.
    Wilson, Ian A.
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2010, 66 : 1167 - 1173
123