1dy6

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[[Image:1dy6.gif|left|200px]]<br /><applet load="1dy6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dy6.gif|left|200px]]
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caption="1dy6, resolution 2.13&Aring;" />
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'''STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1'''<br />
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{{Structure
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|PDB= 1dy6 |SIZE=350|CAPTION= <scene name='initialview01'>1dy6</scene>, resolution 2.13&Aring;
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|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>
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|LIGAND=
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|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]
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|GENE=
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}}
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'''STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY6 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11807251 11807251]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:48 2008''
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''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


PDB ID 1dy6

Drag the structure with the mouse to rotate
, resolution 2.13Å
Sites: and
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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