1bue: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1bue.jpg|left|200px]]
{{Seed}}
[[Image:1bue.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bue|  PDB=1bue  |  SCENE=  }}  
{{STRUCTURE_1bue|  PDB=1bue  |  SCENE=  }}  


'''NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_9756914}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9756914 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9756914}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Class a carbapenemase]]
[[Category: Class a carbapenemase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:58:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:44:18 2008''