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1ac5
From Proteopedia
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| - | [[Image:1ac5.gif|left|200px]]<br /><applet load="1ac5" size=" | + | [[Image:1ac5.gif|left|200px]]<br /><applet load="1ac5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ac5, resolution 2.4Å" /> | caption="1ac5, resolution 2.4Å" /> | ||
'''CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE'''<br /> | '''CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] Known structural/functional Sites: <scene name='pdbsite=176:Member Of Catalytic Triad'>176</scene>, <scene name='pdbsite=383:Member Of Catalytic Triad'>383</scene> and <scene name='pdbsite=448:Member Of Catalytic Triad'>448</scene>. Full crystallographic information is available from [http:// | + | 1AC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] Known structural/functional Sites: <scene name='pdbsite=176:Member+Of+Catalytic+Triad'>176</scene>, <scene name='pdbsite=383:Member+Of+Catalytic+Triad'>383</scene> and <scene name='pdbsite=448:Member+Of+Catalytic+Triad'>448</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AC5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:45 2008'' |
Revision as of 07:29, 3 February 2008
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CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE
Overview
A soluble form of the killer factor and prohormone-processing, carboxypeptidase, "Kex1 delta p," from Saccharomyces cerevisiae, has been, crystallized in 17-22% poly(enthylene glycol) methyl ether (average M(r) =, 5,000), 100 mM ammonium acetate, 5% glycerol, pH 6.5, at 20 degrees C. A, native data set (2.8 A resolution) and four derivative data sets (3.0-3.2, A resolution) were collected at the Photon Factory (lambda = 1.0 A). The, crystals belong to space group P2(1)2(1)2(1) with a =56.6 A, b = 84.0 A, c, = 111.8 A. Freezing a Kex1 delta p crystal has facilitated the collection, of a 2.4-A data set using a rotating anode source (lambda = 1.5418 A)., Molecular replacement models have been built based on the structures of, wheat serine carboxypeptidase (CPDW-II; Liao DI et al., 1992, Biochemistry, 31:9796-9812) and yeast carboxypeptidase Y.
About this Structure
1AC5 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Carboxypeptidase D, with EC number 3.4.16.6 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae., Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M, Protein Sci. 1996 Feb;5(2):395-7. PMID:8745419
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