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1p10
From Proteopedia
Revision as of 19:55, 28 September 2014 by OCA (Talk | contribs)
1p10 is a 2 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Bone R, Silen JL, Agard DA. Structural plasticity broadens the specificity of an engineered protease. Nature. 1989 May 18;339(6221):191-5. PMID:2716847 doi:http://dx.doi.org/10.1038/339191a0
