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1p10

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[[Image:1p10.gif|left|200px]]
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{{STRUCTURE_1p10| PDB=1p10 | SCENE= }}
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'''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''
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===STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES===
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==Overview==
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The substrate specificity of alpha-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.
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(as it appears on PubMed at http://www.pubmed.gov), where 2716847 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2716847}}
==About this Structure==
==About this Structure==
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[[Category: Agard, D A.]]
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[[Category: Bone, R.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:32:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:01:51 2008''

Revision as of 10:01, 27 July 2008

Image:1p10.png

Template:STRUCTURE 1p10

STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES

Template:ABSTRACT PUBMED 2716847

About this Structure

1P10 is a Single protein structure of sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

Reference

Structural plasticity broadens the specificity of an engineered protease., Bone R, Silen JL, Agard DA, Nature. 1989 May 18;339(6221):191-5. PMID:2716847

Page seeded by OCA on Sun Jul 27 13:01:51 2008

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