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1dbi

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[[Image:1dbi.gif|left|200px]]<br /><applet load="1dbi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dbi.gif|left|200px]]
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caption="1dbi, resolution 1.8&Aring;" />
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'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''<br />
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{{Structure
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|PDB= 1dbi |SIZE=350|CAPTION= <scene name='initialview01'>1dbi</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE'''
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==Overview==
==Overview==
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==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 <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].
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1DBI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBI OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10588904 10588904]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10588904 10588904]
[[Category: Bacillus sp.]]
[[Category: Bacillus sp.]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[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''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:49 2008''

Revision as of 08:35, 20 March 2008

Image:1dbi.gif


PDB ID 1dbi

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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.. 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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