1dy6: Difference between revisions
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[[Image:1dy6.gif|left|200px]] | [[Image:1dy6.gif|left|200px]] | ||
'''STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1''' | {{Structure | ||
|PDB= 1dy6 |SIZE=350|CAPTION= <scene name='initialview01'>1dy6</scene>, resolution 2.13Å | |||
|SITE= <scene name='pdbsite=ASA:Beta-Lactam+Binding+Site,+Chain+A'>ASA</scene> and <scene name='pdbsite=ASB:Beta-Lactam+Binding+Site,+Chain+B'>ASB</scene> | |||
|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= | |||
}} | |||
'''STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DY6 is a [ | 1DY6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY6 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11807251 11807251] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
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[[Category: lactamase]] | [[Category: lactamase]] | ||
''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 10:46:20 2008'' | ||
Revision as of 08:46, 20 March 2008
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| 1dy6, resolution 2.13Å | |||||||||||||
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| Sites: | ASA and ASB | ||||||||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1
Overview
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.
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
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