1j71

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(New page: 200px<br /><applet load="1j71" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j71, resolution 1.80&Aring;" /> '''Structure of the ext...)
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[[Image:1j71.jpg|left|200px]]<br /><applet load="1j71" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j71, resolution 1.80&Aring;" />
caption="1j71, resolution 1.80&Aring;" />
'''Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.'''<br />
'''Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.'''<br />
==Overview==
==Overview==
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The crystal structure of the secreted aspartic proteinase from Candida, tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The, classic aspartic proteinase bilobal structure and domain topology is, conserved in SAPT, with the substrate binding cleft situated between the, two domains. Structural comparisons made with pepsin indicate that, insertions and deletions in the primary sequence modify the SAPT structure, to create a more spacious substrate binding cleft with altered, specificity. An unexpected tetrapeptide has been found to occupy binding, sites S1'-S3', and this suggests the order of release of peptide products, in the catalytic mechanism of these enzymes. Structural features are, considered with regard to previous substrate specificity data.
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The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data.
==About this Structure==
==About this Structure==
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1J71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] and [http://en.wikipedia.org/wiki/Unidentified Unidentified] with EOH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J71 OCA].
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1J71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] and [http://en.wikipedia.org/wiki/Unidentified Unidentified] with <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J71 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Unidentified]]
[[Category: Unidentified]]
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[[Category: Foundling, S.I.]]
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[[Category: Foundling, S I.]]
[[Category: Monod, M.]]
[[Category: Monod, M.]]
[[Category: Symersky, J.]]
[[Category: Symersky, J.]]
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[[Category: sapt1]]
[[Category: sapt1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:58:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:24 2008''

Revision as of 11:19, 21 February 2008


1j71, resolution 1.80Å

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Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

Overview

The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data.

About this Structure

1J71 is a Single protein structure of sequence from Candida tropicalis and Unidentified with as ligand. Active as Candidapepsin, with EC number 3.4.23.24 Full crystallographic information is available from OCA.

Reference

High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast., Symersky J, Monod M, Foundling SI, Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526

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