1p09
From Proteopedia
(New page: 200px<br /><applet load="1p09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p09, resolution 2.20Å" /> '''STRUCTURAL PLASTICIT...) |
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| - | [[Image:1p09.gif|left|200px]]<br /><applet load="1p09" size=" | + | [[Image:1p09.gif|left|200px]]<br /><applet load="1p09" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p09, resolution 2.20Å" /> | caption="1p09, resolution 2.20Å" /> | ||
'''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''<br /> | '''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The substrate specificity of alpha-lytic protease has been changed | + | 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== | ==About this Structure== | ||
| - | 1P09 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1P09 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P09 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysobacter enzymogenes]] | [[Category: Lysobacter enzymogenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Agard, D | + | [[Category: Agard, D A.]] |
[[Category: Bone, R.]] | [[Category: Bone, R.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:37 2008'' |
Revision as of 12:23, 21 February 2008
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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 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 Thu Feb 21 14:23:37 2008
