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| - | [[Image:1dy6.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dy6.png|left|200px]] |
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| | {{STRUCTURE_1dy6| PDB=1dy6 | SCENE= }} | | {{STRUCTURE_1dy6| PDB=1dy6 | SCENE= }} |
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| - | '''STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1'''
| + | ===STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1=== |
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| - | ==Overview==
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| - | The structure of the beta-lactamase SME-1 from Serratia marcescens, a class A enzyme characterized by its significant activity against imipenem, has been determined to 2.13 A resolution. The overall structure of SME-1 is similar to that of other class A beta-lactamases. In the active-site cavity, most of the residues found in SME-1 are conserved among class A beta-lactamases, except at positions 104, 105 and 237, where a tyrosine, a histidine and a serine are found, respectively, and at position 238, which is occupied by a cysteine forming a disulfide bridge with the other cysteine residue located at position 69. The crucial role played by this disulfide bridge in SME-1 was confirmed by site-directed mutagenesis of Cys69 to Ala, which resulted in a mutant unable to confer resistance to imipenem and all other beta-lactam antibiotics tested. Another striking structural feature found in SME-1 was the short distance separating the side chains of the active serine residue at position 70 and the strictly conserved glutamate at position 166, which is up to 1.4 A shorter in SME-1 compared with other class A beta-lactamases. Consequently, the SME-1 structure cannot accommodate the essential catalytic water molecule found between Ser70 and Glu166 in the other class A beta-lactamases described so far, suggesting that a significant conformational change may be necessary in SME-1 to properly position the hydrolytic water molecule involved in the hydrolysis of the acyl-enzyme intermediate.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11807251}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11807251 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11807251}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Imipenem]] | | [[Category: Imipenem]] |
| | [[Category: Lactamase]] | | [[Category: Lactamase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:25:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:47:51 2008'' |
Revision as of 20:47, 30 June 2008
Template:STRUCTURE 1dy6
STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1
Template:ABSTRACT PUBMED 11807251
About this Structure
1DY6 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.
Reference
Structure of the imipenem-hydrolyzing class A beta-lactamase SME-1 from Serratia marcescens., Sougakoff W, L'Hermite G, Pernot L, Naas T, Guillet V, Nordmann P, Jarlier V, Delettre J, Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):267-74. Epub 2002, Jan 24. PMID:11807251
Page seeded by OCA on Mon Jun 30 23:47:51 2008
