1.37 Å Crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli

被引：2
|
作者：
Tang, Qun [1 ,2 ]
Liu, Yan-Ping [2 ]
Ren, Zheng-Guang [1 ]
Yan, Xiao-Xue [2 ]
Zhang, Li-Qun [1 ]
机构：
[1] China Agr Univ, Dept Plant Pathol, Beijing 100193, Peoples R China
[2] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2013年 / 81卷 / 08期
基金：
中国国家自然科学基金;
关键词：
pectate lyase; pathogenic factor; Acidovorax citrulli; crystal structure; right-handed; -helix; SEQUENCE ALIGNMENT; BINDING;
D O I：
10.1002/prot.24298
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：
Pectates lyase (Pel) plays an important role in bacteria pathogenicity. The crystal structure of Pel from Acidovorax citrulli (AcPel) has been solved to 1.37 angstrom resolution. AcPel belongs to the polysaccharide lyase family 1 (PL1), which has a characteristic right-handed -helix fold. AcPel is similar with other Pels in the PL1 family, but also shows some differences at the substrate binding site. Proteins 2013; 81:1485-1490. (c) 2013 Wiley Periodicals, Inc.
引用
收藏
页码：1485 / 1490
页数：6
相关论文
共 50 条
  • [1] PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF A PLANT PATHOGENIC FACTOR - PECTATE LYASE
    KIM, CY
    MOSSER, V
    KEEN, N
    JURNAK, F
    JOURNAL OF MOLECULAR BIOLOGY, 1989, 208 (02) : 365 - 367
  • [2] The crystal structure of pectate lyase Pel9A from Erwinia chrysanthemi
    Jenkins, J
    Shevchik, VE
    Hugouvieux-Cotte-Pattat, N
    Pickersgill, RW
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (10) : 9139 - 9145
  • [3] PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF THE PLANT PATHOGENIC FACTOR, PECTATE LYASE-C FROM ERWINIA CHRYSANTHEMI
    YODER, MD
    DECHAINE, DA
    JURNAK, F
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1990, 265 (20) : 11429 - 11431
  • [4] CRYSTAL STRUCTURE OF THE THERMOSTABLE PECTATE LYASE FROM BACILLUS SP. TS 47
    Nakaniwa, T.
    Ishii, K.
    Tada, T.
    Takao, M.
    Sakai, T.
    Nishimura, K.
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2002, 58 : C109 - C109
  • [5] STRUCTURE OF A NOVEL PECTATE LYASE FROM AZOSPIRILLUM IRAKENSE
    de Armas, H. Novoa
    Rabijns, A.
    Verboven, C.
    Desair, J.
    Broeck, A. Vande
    Vanderleyden, J.
    De Ranter, C.
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2002, 58 : C110 - C110
  • [6] Multi-factor regulation of pectate lyase secretion by Colletotrichum gloeosporioides pathogenic on avocado fruits
    Miyara, I.
    Shafran, H.
    Haimovich, H. Kramer
    Rollins, J.
    Sherman, A.
    Prusky, D.
    MOLECULAR PLANT PATHOLOGY, 2008, 9 (03) : 281 - 291
  • [7] Insights from comparative analyses between the genomes of two model strains of the cucurbit pathogenic bacterium Acidovorax citrulli
    Burdman, S.
    Eckshtain-Levi, N.
    Shkedy, D.
    Gershovits, M.
    da Silva, G. Mateus
    Tamir-Ariel, D.
    Walcott, R.
    Pupko, T.
    PHYTOPATHOLOGY, 2016, 106 (12) : 26 - 27
  • [8] The crystal structure of pectate lyase PelI from soft rot pathogen Erwinia chrysanthemi in complex with its substrate
    Creze, Christophe
    Castang, Sandra
    Derivery, Emmanuel
    Haser, Richard
    Hugouvieux-Cotte-Pattat, Nicole
    Shevchik, Vladimir E.
    Gouet, Patrice
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (26) : 18260 - 18268
  • [9] THE 3-DIMENSIONAL STRUCTURE OF PECTATE LYASE-E, A PLANT VIRULENCE FACTOR FROM ERWINIA-CHRYSANTHEMI
    LIETZKE, SE
    YODER, MD
    KEEN, NT
    JURNAK, F
    PLANT PHYSIOLOGY, 1994, 106 (03) : 849 - 862
  • [10] NEW DOMAIN MOTIF - THE STRUCTURE OF PECTATE LYASE-C, A SECRETED PLANT VIRULENCE FACTOR
    YODER, MD
    KEEN, NT
    JURNAK, F
    SCIENCE, 1993, 260 (5113) : 1503 - 1507
12345