1a7t

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{{STRUCTURE_1a7t| PDB=1a7t | SCENE= }}
{{STRUCTURE_1a7t| PDB=1a7t | SCENE= }}
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'''METALLO-BETA-LACTAMASE WITH MES'''
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===METALLO-BETA-LACTAMASE WITH MES===
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==Overview==
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As part of a structure-aided effort to design clinically useful inhibitors of metallo-beta-lactamases, the X-ray crystal structure of a complex between the metallo-beta-lactamase from Bacteroides fragilis and 4-morpholinoethanesulfonic acid (MES) has been determined and a model for the structure has been refined to a crystallographic R-factor of 0.151 for data between 10.0- and 1.85-A resolution. Although the binding of MES was an adventitious result of the use of MES as a buffer in the crystallization mixture, MES was subsequently shown to be a competitive inhibitor of the enzyme, with a Ki of 23 +/- 5 mM. MES binds in the same fashion to both of the molecules in the crystallographic asymmetric unit; both direct and solvent-mediated hydrogen bonds to the protein and to the binuclear zinc cluster are observed, involving the oxygens of the sulfonic acid group and the nitrogen of the morpholino ring. In addition, there are hydrophobic interactions between the morpholino ring and residues in the flexible beta-strand of the enzyme between residues 26 and 36. Comparison of this structure with the previously reported unliganded structures of the same enzyme [Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O. (1996) Structure 4, 823-836; Carfi, A., Duee, E., Paul-Soto, R., Galleni, M., Frere, J. -M., and Dideberg, O. (1998) Acta Crystallogr. D54, 47-57] reveals that although the overall conservation of structure in the three different crystal lattices is very high, binding of MES is correlated with a significant change in the conformation of this beta-strand. The flexibility of this beta-strand will be an important consideration in the design of inhibitors of the metallo-beta-lactamases.
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(as it appears on PubMed at http://www.pubmed.gov), where 9578564 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9578564}}
==About this Structure==
==About this Structure==
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[[Category: Metallo beta-lactamase]]
[[Category: Metallo beta-lactamase]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:56:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:19:56 2008''

Revision as of 13:20, 30 June 2008

Image:1a7t.png

Template:STRUCTURE 1a7t

METALLO-BETA-LACTAMASE WITH MES

Template:ABSTRACT PUBMED 9578564

About this Structure

1A7T is a Single protein structure of sequence from Bacteroides fragilis. Full crystallographic information is available from OCA.

Reference

Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution., Fitzgerald PM, Wu JK, Toney JH, Biochemistry. 1998 May 12;37(19):6791-800. PMID:9578564

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