1jwp

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[[Image:1jwp.jpg|left|200px]]
[[Image:1jwp.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1jwp |SIZE=350|CAPTION= <scene name='initialview01'>1jwp</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1jwp", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= bla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1jwp| PDB=1jwp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwp OCA], [http://www.ebi.ac.uk/pdbsum/1jwp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jwp RCSB]</span>
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}}
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'''Structure of M182T mutant of TEM-1 beta-lactamase'''
'''Structure of M182T mutant of TEM-1 beta-lactamase'''
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[[Category: Shoichet, B K.]]
[[Category: Shoichet, B K.]]
[[Category: Wang, X.]]
[[Category: Wang, X.]]
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[[Category: antibiotic resistance]]
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[[Category: Antibiotic resistance]]
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[[Category: beta-lactamase]]
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[[Category: Beta-lactamase]]
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[[Category: evolution]]
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[[Category: Evolution]]
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[[Category: protein stability]]
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[[Category: Protein stability]]
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[[Category: tem-1]]
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[[Category: Tem-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:01:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:09 2008''
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Revision as of 19:01, 2 May 2008

Image:1jwp.jpg

Template:STRUCTURE 1jwp

Structure of M182T mutant of TEM-1 beta-lactamase


Overview

Pressured by antibiotic use, resistance enzymes have been evolving new activities. Does such evolution have a cost? To investigate this question at the molecular level, clinically isolated mutants of the beta-lactamase TEM-1 were studied. When purified, mutant enzymes had increased activity against cephalosporin antibiotics but lost both thermodynamic stability and kinetic activity against their ancestral targets, penicillins. The X-ray crystallographic structures of three mutant enzymes were determined. These structures suggest that activity gain and stability loss is related to an enlarged active site cavity in the mutant enzymes. In several clinically isolated mutant enzymes, a secondary substitution is observed far from the active site (Met182-->Thr). This substitution had little effect on enzyme activity but restored stability lost by substitutions near the active site. This regained stability conferred an advantage in vivo. This pattern of stability loss and restoration may be common in the evolution of new enzyme activity.

About this Structure

1JWP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs., Wang X, Minasov G, Shoichet BK, J Mol Biol. 2002 Jun 28;320(1):85-95. PMID:12079336 Page seeded by OCA on Fri May 2 22:01:11 2008

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