1P10

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

Summary for 1P10

Entry DOI	10.2210/pdb1p10/pdb
Related PRD ID	PRD_000316
Descriptor	ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR, SULFATE ION, ... (4 entities in total)
Functional Keywords	serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Lysobacter enzymogenes
Total number of polymer chains	2
Total formula weight	20381.40
Authors	Bone, R.,Agard, D.A. (deposition date: 1989-04-24, release date: 1990-04-15, Last modification date: 2024-06-05)
Primary citation	Bone, R.,Silen, J.L.,Agard, D.A. Structural plasticity broadens the specificity of an engineered protease. Nature, 339:191-195, 1989 Cited by PubMed Abstract: 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. PubMed: 2716847 DOI: 10.1038/339191a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.25 Å)

Structure validation