Literature DB >> 19407375

Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.

Akihiro Yamamura1, Akitoshi Okada, Yasuhiro Kameda, Jun Ohtsuka, Noriko Nakagawa, Akio Ebihara, Koji Nagata, Masaru Tanokura.   

Abstract

TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

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Year:  2009        PMID： 19407375      PMCID： PMC2675583          DOI： 10.1107/S174430910901361X

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  17 in total

1.  An approach to multi-copy search in molecular replacement.

Authors:  A Vagin; A Teplyakov
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2000-12

2.  Refinement of macromolecular structures by the maximum-likelihood method.

Authors:  G N Murshudov; A A Vagin; E J Dodson
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1997-05-01

3.  Crystal structure of TTHA1429, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.

Authors:  Akihiro Yamamura; Jun Ohtsuka; Keiko Kubota; Yoshihiro Agari; Akio Ebihara; Noriko Nakagawa; Koji Nagata; Masaru Tanokura
Journal:  Proteins       Date:  2008-12

4.  Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.

Authors:  A D Cameron; M Ridderström; B Olin; B Mannervik
Journal:  Structure       Date:  1999-09-15       Impact factor: 5.006

5.  Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism.

Authors:  Anna M Davies; Rodolfo M Rasia; Alejandro J Vila; Brian J Sutton; Stella M Fabiane
Journal:  Biochemistry       Date:  2005-03-29       Impact factor: 3.162

6.  Dali: a network tool for protein structure comparison.

Authors:  L Holm; C Sander
Journal:  Trends Biochem Sci       Date:  1995-11       Impact factor: 13.807

7.  Structure of an ETHE1-like protein from Arabidopsis thaliana.

Authors:  Jason G McCoy; Craig A Bingman; Eduard Bitto; Meghan M Holdorf; Christopher A Makaroff; George N Phillips
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2006-08-19

8.  Automated MAD and MIR structure solution.

Authors:  T C Terwilliger; J Berendzen
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1999-04

Review 9.  Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily.

Authors:  Carine Bebrone
Journal:  Biochem Pharmacol       Date:  2007-06-02       Impact factor: 5.858

10.  The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.

Authors:  A Carfi; S Pares; E Duée; M Galleni; C Duez; J M Frère; O Dideberg
Journal:  EMBO J       Date:  1995-10-16       Impact factor: 11.598
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  4 in total

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Journal:  J Mol Evol       Date:  2013-08-10       Impact factor: 2.395

2.  Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase.

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3.  LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria.

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Journal:  BMC Genomics       Date:  2010-11-23       Impact factor: 3.969

4.  Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure determination, table of crystallographic data, table of crystallographic parameters and refinement statistics, figures showing binding mode and distances, procedures for mass spectrometry measurements, differential scanning fluorimetry measurements, stopped-flow measurements and other kinetics measurements. See DOI: 10.1039/c4sc01752hClick here for additional data file.

Authors:  Jürgen Brem; Weston B Struwe; Anna M Rydzik; Hanna Tarhonskaya; Inga Pfeffer; Emily Flashman; Sander S van Berkel; James Spencer; Timothy D W Claridge; Michael A McDonough; Justin L P Benesch; Christopher J Schofield
Journal:  Chem Sci       Date:  2014-11-04       Impact factor: 9.825
  4 in total

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