1p09

From Proteopedia

Revision as of 21:13, 20 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1p09, resolution 2.20Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1P09 is a Single protein structure of sequence from Lysobacter enzymogenes with SO4 as ligand. Active as Alpha-lytic endopeptidase, with EC number 3.4.21.12 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 Tue Nov 20 23:20:19 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools