1dbi

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(New page: 200px<br /><applet load="1dbi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dbi, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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caption="1dbi, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''<br />
'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''<br />
==Overview==
==Overview==
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Proteins of the subtilisin superfamily (subtilases) are widely distributed, through many living species, where they perform a variety of processing, functions. They are also used extensively in industry. In many of these, enzymes, bound calcium ions play a key role in protecting against, autolysis and thermal denaturation. We have determined the crystal, structure of a highly thermostable protease from Bacillus sp. Ak.1 that is, strongly stabilized by calcium. The crystal structure, determined at 1.8 A, resolution (R=0. 182, Rfree=0.247), reveals the presence of four bound, cations, three Ca(2+) and one Na(+). Two of the Ca(2+) binding sites, Ca-1, and Ca-2, correspond to sites also found in thermitase and the mesophilic, subtilisins. The third calcium ion, however, is at a novel site that is, created by two key amino acid substitutions near Ca-1, and has not been, observed in any other subtilase. This site, acting cooperatively with, Ca-1, appears to give substantially enhanced thermostability, compared, with thermitase. Comparisons with the mesophilic subtilisins also point to, the importance of aromatic clusters, reduced hydrophobic surface and, constrained N and C termini in enhancing the thermostability of thermitase, and Ak.1 protease. The Ak.1 protease also contains an unusual Cys-X-Cys, disulfide bridge that modifies the active site cleft geometry.
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Proteins of the subtilisin superfamily (subtilases) are widely distributed through many living species, where they perform a variety of processing functions. They are also used extensively in industry. In many of these enzymes, bound calcium ions play a key role in protecting against autolysis and thermal denaturation. We have determined the crystal structure of a highly thermostable protease from Bacillus sp. Ak.1 that is strongly stabilized by calcium. The crystal structure, determined at 1.8 A resolution (R=0. 182, Rfree=0.247), reveals the presence of four bound cations, three Ca(2+) and one Na(+). Two of the Ca(2+) binding sites, Ca-1 and Ca-2, correspond to sites also found in thermitase and the mesophilic subtilisins. The third calcium ion, however, is at a novel site that is created by two key amino acid substitutions near Ca-1, and has not been observed in any other subtilase. This site, acting cooperatively with Ca-1, appears to give substantially enhanced thermostability, compared with thermitase. Comparisons with the mesophilic subtilisins also point to the importance of aromatic clusters, reduced hydrophobic surface and constrained N and C termini in enhancing the thermostability of thermitase and Ak.1 protease. The Ak.1 protease also contains an unusual Cys-X-Cys disulfide bridge that modifies the active site cleft geometry.
==About this Structure==
==About this Structure==
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1DBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DBI OCA].
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1DBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBI OCA].
==Reference==
==Reference==
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[[Category: Bacillus sp.]]
[[Category: Bacillus sp.]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, E.N.]]
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[[Category: Baker, E N.]]
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[[Category: Baker, H.M.]]
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[[Category: Baker, H M.]]
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[[Category: Daniel, R.M.]]
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[[Category: Daniel, R M.]]
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[[Category: Smith, C.A.]]
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[[Category: Smith, C A.]]
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[[Category: Toogood, H.S.]]
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[[Category: Toogood, H S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: NA]]
[[Category: NA]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:56 2008''

Revision as of 10:14, 21 February 2008


1dbi, resolution 1.8Å

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CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE

Overview

Proteins of the subtilisin superfamily (subtilases) are widely distributed through many living species, where they perform a variety of processing functions. They are also used extensively in industry. In many of these enzymes, bound calcium ions play a key role in protecting against autolysis and thermal denaturation. We have determined the crystal structure of a highly thermostable protease from Bacillus sp. Ak.1 that is strongly stabilized by calcium. The crystal structure, determined at 1.8 A resolution (R=0. 182, Rfree=0.247), reveals the presence of four bound cations, three Ca(2+) and one Na(+). Two of the Ca(2+) binding sites, Ca-1 and Ca-2, correspond to sites also found in thermitase and the mesophilic subtilisins. The third calcium ion, however, is at a novel site that is created by two key amino acid substitutions near Ca-1, and has not been observed in any other subtilase. This site, acting cooperatively with Ca-1, appears to give substantially enhanced thermostability, compared with thermitase. Comparisons with the mesophilic subtilisins also point to the importance of aromatic clusters, reduced hydrophobic surface and constrained N and C termini in enhancing the thermostability of thermitase and Ak.1 protease. The Ak.1 protease also contains an unusual Cys-X-Cys disulfide bridge that modifies the active site cleft geometry.

About this Structure

1DBI is a Single protein structure of sequence from Bacillus sp. with and as ligands. Full crystallographic information is available from OCA.

Reference

Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution., Smith CA, Toogood HS, Baker HM, Daniel RM, Baker EN, J Mol Biol. 1999 Dec 10;294(4):1027-40. PMID:10588904

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