1p09

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[[Image:1p09.gif|left|200px]]
[[Image:1p09.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1p09 |SIZE=350|CAPTION= <scene name='initialview01'>1p09</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1p09", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1p09| PDB=1p09 | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''
'''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''
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[[Category: Agard, D A.]]
[[Category: Agard, D A.]]
[[Category: Bone, R.]]
[[Category: Bone, R.]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:30:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:52:52 2008''
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Revision as of 01:30, 3 May 2008

Image:1p09.gif

Template:STRUCTURE 1p09

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 Sat May 3 04:30:45 2008

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OCA

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