1bue
From Proteopedia
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| - | [[Image:1bue.jpg|left|200px]] | + | [[Image:1bue.jpg|left|200px]] |
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| - | '''NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE''' | + | {{Structure |
| + | |PDB= 1bue |SIZE=350|CAPTION= <scene name='initialview01'>1bue</scene>, resolution 1.64Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BUE is a [ | + | 1BUE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUE OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity., Swaren P, Maveyraud L, Raquet X, Cabantous S, Duez C, Pedelacq JD, Mariotte-Boyer S, Mourey L, Labia R, Nicolas-Chanoine MH, Nordmann P, Frere JM, Samama JP, J Biol Chem. 1998 Oct 9;273(41):26714-21. PMID:[http:// | + | X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity., Swaren P, Maveyraud L, Raquet X, Cabantous S, Duez C, Pedelacq JD, Mariotte-Boyer S, Mourey L, Labia R, Nicolas-Chanoine MH, Nordmann P, Frere JM, Samama JP, J Biol Chem. 1998 Oct 9;273(41):26714-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9756914 9756914] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Enterobacter cloacae]] | [[Category: Enterobacter cloacae]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:55 2008'' |
Revision as of 08:16, 20 March 2008
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| , resolution 1.64Å | |||||||
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| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE
Overview
The treatment of infectious diseases by penicillin and cephalosporin antibiotics is continuously challenged by the emergence and the dissemination of the numerous TEM and SHV mutant beta-lactamases with extended substrate profiles. These class A beta-lactamases nevertheless remain inefficient against carbapenems, the most effective antibiotics against clinically relevant pathogens. A new member of this enzyme class, NMC-A, was recently reported to hydrolyze at high rates, and hence destroy, all known beta-lactam antibiotics, including carbapenems and cephamycins. The crystal structure of NMC-A was solved to 1.64-A resolution, and reveals modifications in the topology of the substrate-binding site. While preserving the geometry of the essential catalytic residues, the active site of the enzyme presents a disulfide bridge between residues 69 and 238, and certain other structural differences compared with the other beta-lactamases. These unusual features in class A beta-lactamases involve amino acids that participate in enzyme-substrate interactions, which suggested that these structural factors should be related to the very broad substrate specificity of this enzyme. The comparison of the NMC-A structure with those of other class A enzymes and enzyme-ligand complexes, indicated that the position of Asn-132 in NMC-A provides critical additional space in the region of the protein where the poorer substrates for class A beta-lactamases, such as cephamycins and carbapenems, need to be accommodated.
About this Structure
1BUE is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.
Reference
X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity., Swaren P, Maveyraud L, Raquet X, Cabantous S, Duez C, Pedelacq JD, Mariotte-Boyer S, Mourey L, Labia R, Nicolas-Chanoine MH, Nordmann P, Frere JM, Samama JP, J Biol Chem. 1998 Oct 9;273(41):26714-21. PMID:9756914
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