Active site loop of metallo-β-lactamases tunes metal site coordination and affects catalysis by second sphere interactions

被引：0
|
作者：
Palacios, Antonela R. [1 ]
Mojica, Maria F. [2 ,3 ]
Taracila, Magdalena A. [2 ,3 ]
Bethel, Christopher R. [3 ]
Giannini, Estefania [1 ]
Llarrull, Leticia I. [1 ]
Bonomo, Robert A. [2 ,3 ]
Vila, Alejandro J. [1 ]
机构：
[1] UNR, CONICET, IBR, Inst Biol Mol & Celular Rosario, Rosario, Santa Fe, Argentina
[2] CWRU, Cleveland, OH USA
[3] VAMC, Cleveland, OH USA
来源：
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2017年 / 22卷
关键词：
Metallo-Beta-Lactamase; Active Site Loop; Second Sphere;
D O I：
暂无
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：
引用
收藏
页码：S128 / S128
页数：1
相关论文
共 40 条
  • [1] Probing the active site and mobile loop of metallo-β-lactamases during catalysis
    Aitha, Mahesh
    Richmond, Timothy K.
    Hu, Zhenxin
    Hetrick, Alyssa
    Reese, Raquel
    McCarrick, Robert
    Tierney, David L.
    Bennett, Brian
    Crowder, Michael W.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2013, 246
  • [2] Evidence of Adaptability in Metal Coordination Geometry and Active-Site Loop Conformation among B1 Metallo-β-lactamases
    Gonzalez, Javier M.
    Buschiazzo, Alejandro
    Vila, Alejandro J.
    BIOCHEMISTRY, 2010, 49 (36) : 7930 - 7938
  • [3] The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop
    Palacios, Antonela R.
    Mojica, Maria F.
    Giannini, Estefania
    Taracila, Magdalena A.
    Bethel, Christopher R.
    Alzari, Pedro M.
    Otero, Lisandro H.
    Klinke, Sebastian
    Llarrull, Leticia I.
    Bonomo, Robert A.
    Vila, Alejandro J.
    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2019, 63 (01)
  • [4] Analysis of the importance of the metallo-β-lactamase active site loop in substrate binding and catalysis
    Moali, C
    Anne, C
    Lamotte-Brasseur, J
    Groslambert, S
    Devreese, B
    Van Beeumen, J
    Galleni, M
    Frère, JM
    CHEMISTRY & BIOLOGY, 2003, 10 (04): : 319 - 329
  • [5] Ceftibuten stability to active-site serine and metallo-β-lactamases
    Perilli, M
    Segatore, B
    Franceschini, N
    Gizzi, G
    Mancinelli, A
    Caravelli, B
    Setacci, D
    Tavio-Perez, MD
    Bianchi, B
    Amicosante, G
    INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS, 2001, 17 (01) : 45 - 50
  • [6] Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition
    Elena O. Levina
    Maria G. Khrenova
    Biochemistry (Moscow), 2021, 86 : S24 - S37
  • [7] Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition
    Levina, Elena O.
    Khrenova, Maria G.
    BIOCHEMISTRY-MOSCOW, 2021, 86 (SUPPL 1) : S24 - S37
  • [8] Binding of β-Lactam Antibiotics to a Bioinspired Dizinc Complex Reminiscent of the Active Site of Metallo-β-lactamases
    Woeckel, Simone
    Galezowska, Joanna
    Dechert, Sebastian
    Meyer, Franc
    INORGANIC CHEMISTRY, 2012, 51 (04) : 2486 - 2493
  • [9] Noncovalent interactions between the second coordination sphere and the active site of [NiFeSe] hydrogenase
    Vedha, Swaminathan Angeline
    Velmurugan, Gunasekaran
    Venuvanalingam, Ponnambalam
    RSC ADVANCES, 2016, 6 (85) : 81636 - 81646
  • [10] Gating interactions steer loop conformational changes in the active site of the L1 metallo-β-lactamase
    Zhao, Zhuoran
    Shen, Xiayu
    Chen, Shuang
    Gu, Jing
    Wang, Haun
    Mojica, Maria F.
    Samanta, Moumita
    Bhowmik, Debsindhu
    Vila, Alejandro J.
    Bonomo, Robert A.
    Haider, Shozeb
    ELIFE, 2023, 12
1234