1l0g

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[[Image:1l0g.gif|left|200px]]
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{{STRUCTURE_1l0g| PDB=1l0g | SCENE= }}
{{STRUCTURE_1l0g| PDB=1l0g | SCENE= }}
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'''X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase'''
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===X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase===
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==Overview==
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The structures of enzymes reflect two tendencies that appear opposed. On one hand, they fold into compact, stable structures; on the other hand, they bind a ligand and catalyze a reaction. To be stable, enzymes fold to maximize favorable interactions, forming a tightly packed hydrophobic core, exposing hydrophilic groups, and optimizing intramolecular hydrogen-bonding. To be functional, enzymes carve out an active site for ligand binding, exposing hydrophobic surface area, clustering like charges, and providing unfulfilled hydrogen bond donors and acceptors. Using AmpC beta-lactamase, an enzyme that is well-characterized structurally and mechanistically, the relationship between enzyme stability and function was investigated by substituting key active-site residues and measuring the changes in stability and activity. Substitutions of catalytic residues Ser64, Lys67, Tyr150, Asn152, and Lys315 decrease the activity of the enzyme by 10(3)-10(5)-fold compared to wild-type. Concomitantly, many of these substitutions increase the stability of the enzyme significantly, by up to 4.7kcal/mol. To determine the structural origins of stabilization, the crystal structures of four mutant enzymes were determined to between 1.90A and 1.50A resolution. These structures revealed several mechanisms by which stability was increased, including mimicry of the substrate by the substituted residue (S64D), relief of steric strain (S64G), relief of electrostatic strain (K67Q), and improved polar complementarity (N152H). These results suggest that the preorganization of functionality characteristic of active sites has come at a considerable cost to enzyme stability. In proteins of unknown function, the presence of such destabilized regions may indicate the presence of a binding site.
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The line below this paragraph, {{ABSTRACT_PUBMED_12144785}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12144785 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12144785}}
==About this Structure==
==About this Structure==
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[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Mutant enzyme]]
[[Category: Mutant enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:24:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:25:46 2008''

Revision as of 08:25, 2 July 2008

Image:1l0g.png

Template:STRUCTURE 1l0g

X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase

Template:ABSTRACT PUBMED 12144785

About this Structure

1L0G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural bases of stability-function tradeoffs in enzymes., Beadle BM, Shoichet BK, J Mol Biol. 2002 Aug 9;321(2):285-96. PMID:12144785

Page seeded by OCA on Wed Jul 2 11:25:46 2008

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