1ll9: Difference between revisions
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[[Image:1ll9.gif|left|200px]] | [[Image:1ll9.gif|left|200px]] | ||
'''Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin''' | {{Structure | ||
|PDB= 1ll9 |SIZE=350|CAPTION= <scene name='initialview01'>1ll9</scene>, resolution 1.87Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=AXL:2-{1-[2-AMINO-2-(4-HYDROXY-PHENYL)-ACETYLAMINO]-2-OXO-ETHYL}-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC ACID'>AXL</scene> | |||
|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= ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LL9 is a [ | 1LL9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL9 OCA]. | ||
==Reference== | ==Reference== | ||
Using steric hindrance to design new inhibitors of class C beta-lactamases., Trehan I, Morandi F, Blaszczak LC, Shoichet BK, Chem Biol. 2002 Sep;9(9):971-80. PMID:[http:// | Using steric hindrance to design new inhibitors of class C beta-lactamases., Trehan I, Morandi F, Blaszczak LC, Shoichet BK, Chem Biol. 2002 Sep;9(9):971-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12323371 12323371] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: serine]] | [[Category: serine]] | ||
''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 12:32:11 2008'' | ||
Revision as of 13:32, 20 March 2008
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| , resolution 1.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ampC (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With Amoxicillin
OverviewOverview
beta-lactamases confer resistance to beta-lactam antibiotics such as penicillins and cephalosporins. However, beta-lactams that form an acyl-intermediate with the enzyme but subsequently are hindered from forming a catalytically competent conformation seem to be inhibitors of beta-lactamases. This inhibition may be imparted by specific groups on the ubiquitous R(1) side chain of beta-lactams, such as the 2-amino-4-thiazolyl methoxyimino (ATMO) group common among third-generation cephalosporins. Using steric hindrance of deacylation as a design guide, penicillin and carbacephem substrates were converted into effective beta-lactamase inhibitors and antiresistance antibiotics. To investigate the structural bases of inhibition, the crystal structures of the acyl-adducts of the penicillin substrate amoxicillin and the new analogous inhibitor ATMO-penicillin were determined. ATMO-penicillin binds in a catalytically incompetent conformation resembling that adopted by third-generation cephalosporins, demonstrating the transferability of such sterically hindered groups in inhibitor design.
About this StructureAbout this Structure
1LL9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Using steric hindrance to design new inhibitors of class C beta-lactamases., Trehan I, Morandi F, Blaszczak LC, Shoichet BK, Chem Biol. 2002 Sep;9(9):971-80. PMID:12323371
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