1fy2
From Proteopedia
(New page: 200px<br /><applet load="1fy2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy2, resolution 1.2Å" /> '''ASPARTYL DIPEPTIDASE'...) |
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| - | [[Image:1fy2.jpg|left|200px]]<br /><applet load="1fy2" size=" | + | [[Image:1fy2.jpg|left|200px]]<br /><applet load="1fy2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fy2, resolution 1.2Å" /> | caption="1fy2, resolution 1.2Å" /> | ||
'''ASPARTYL DIPEPTIDASE'''<br /> | '''ASPARTYL DIPEPTIDASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of Salmonella typhimurium aspartyl | + | The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1FY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1FY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hakansson, K.]] | [[Category: Hakansson, K.]] | ||
| - | [[Category: Miller, C | + | [[Category: Miller, C G.]] |
| - | [[Category: Wang, A | + | [[Category: Wang, A H.J.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: catalytic triad]] | [[Category: catalytic triad]] | ||
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[[Category: strand-helix motif]] | [[Category: strand-helix motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:50 2008'' |
Revision as of 10:43, 21 February 2008
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ASPARTYL DIPEPTIDASE
Overview
The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.
About this Structure
1FY2 is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad., Hakansson K, Wang AH, Miller CG, Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384
Page seeded by OCA on Thu Feb 21 12:43:50 2008
