1p01
From Proteopedia
(New page: 200px<br /><applet load="1p01" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p01, resolution 2.0Å" /> '''SERINE PROTEASE MECHA...) |
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| - | [[Image:1p01.gif|left|200px]]<br /><applet load="1p01" size=" | + | [[Image:1p01.gif|left|200px]]<br /><applet load="1p01" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p01, resolution 2.0Å" /> | caption="1p01, resolution 2.0Å" /> | ||
'''SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID'''<br /> | '''SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the complex formed between alpha-lytic protease, a serine | + | The structure of the complex formed between alpha-lytic protease, a serine protease secreted by Lysobacter enzymogenes, and N-tert-butyloxycarbonylalanylprolylvaline boronic acid (Ki = 0.35 nM) has been studied by X-ray crystallography to a resolution of 2.0 A. The active-site serine forms a covalent, nearly tetrahedral adduct with the boronic acid moiety of the inhibitor. The complex is stabilized by seven hydrogen bonds between the enzyme and inhibitor with additional stabilization arising from van der Waals interactions between enzyme and inhibitor side chains and the burying of 330 A2 of hydrophobic surface area. Hydrogen bonding between Asp-102 and His-57 remains intact in the enzyme-inhibitor complex, and His N epsilon 2 is well positioned to donate its hydrogen to the leaving group. Little change in the positions of protease residues was observed on complex formation (root mean square main chain deviation = 0.13 A), suggesting that in its native state the enzyme is complementary to tetrahedral reaction intermediates or to the nearly tetrahedral transition state for the reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1P01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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:// | + | 1P01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1P01 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Alpha-lytic endopeptidase]] | [[Category: Alpha-lytic endopeptidase]] | ||
[[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 14:23:34 2008'' |
Revision as of 12:23, 21 February 2008
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SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID
Overview
The structure of the complex formed between alpha-lytic protease, a serine protease secreted by Lysobacter enzymogenes, and N-tert-butyloxycarbonylalanylprolylvaline boronic acid (Ki = 0.35 nM) has been studied by X-ray crystallography to a resolution of 2.0 A. The active-site serine forms a covalent, nearly tetrahedral adduct with the boronic acid moiety of the inhibitor. The complex is stabilized by seven hydrogen bonds between the enzyme and inhibitor with additional stabilization arising from van der Waals interactions between enzyme and inhibitor side chains and the burying of 330 A2 of hydrophobic surface area. Hydrogen bonding between Asp-102 and His-57 remains intact in the enzyme-inhibitor complex, and His N epsilon 2 is well positioned to donate its hydrogen to the leaving group. Little change in the positions of protease residues was observed on complex formation (root mean square main chain deviation = 0.13 A), suggesting that in its native state the enzyme is complementary to tetrahedral reaction intermediates or to the nearly tetrahedral transition state for the reaction.
About this Structure
1P01 is a Single protein structure of sequence from [1] with as ligand. Active as Alpha-lytic endopeptidase, with EC number 3.4.21.12 Full crystallographic information is available from OCA.
Reference
Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid., Bone R, Shenvi AB, Kettner CA, Agard DA, Biochemistry. 1987 Dec 1;26(24):7609-14. PMID:3122831
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