1p09
From Proteopedia
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|PDB= 1p09 |SIZE=350|CAPTION= <scene name='initialview01'>1p09</scene>, resolution 2.20Å | |PDB= 1p09 |SIZE=350|CAPTION= <scene name='initialview01'>1p09</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p09 OCA], [http://www.ebi.ac.uk/pdbsum/1p09 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p09 RCSB]</span> | ||
}} | }} | ||
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[[Category: Agard, D A.]] | [[Category: Agard, D A.]] | ||
[[Category: Bone, R.]] | [[Category: Bone, R.]] | ||
| - | [[Category: SO4]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:52:52 2008'' |
Revision as of 19:52, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Alpha-lytic endopeptidase, with EC number 3.4.21.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 30 22:52:52 2008
