1fmx
From Proteopedia
(New page: 200px<br /><applet load="1fmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmx, resolution 2.61Å" /> '''STRUCTURE OF NATIVE ...) |
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| - | [[Image:1fmx.gif|left|200px]]<br /><applet load="1fmx" size=" | + | [[Image:1fmx.gif|left|200px]]<br /><applet load="1fmx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fmx, resolution 2.61Å" /> | caption="1fmx, resolution 2.61Å" /> | ||
'''STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21'''<br /> | '''STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of the native Saccharomyces cerevisiae proteinase A have | + | The structures of the native Saccharomyces cerevisiae proteinase A have been solved by molecular replacement in the monoclinic and trigonal crystal forms and refined at 2.6-2.7A resolution. These structures agree overall with those of other uninhibited aspartic proteinases. However, an unusual orientation for the side chain of Tyr75, a conserved residue on the flexible "flap" that covers the active site and is important for the activity of these enzymes, was found in the trigonal crystals. A similar conformation of Tyr75 occupying the S1 substrate-binding pocket was previously reported only for chymosin (where it was interpreted as representing a "self-inhibited" state of the enzyme), but for no other aspartic proteinases. Since this orientation of Tyr75 has now been seen in the structures of two members of the family of aspartic proteinases, it might indicate that the placement of that residue in the S1 substrate-binding pocket might have some functional significance, analogous to what was seen for self-inhibited structures of serine proteinases. |
==About this Structure== | ==About this Structure== | ||
| - | 1FMX 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/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] Full crystallographic information is available from [http:// | + | 1FMX 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/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gustchina, A.]] | [[Category: Gustchina, A.]] | ||
[[Category: Kay, J.]] | [[Category: Kay, J.]] | ||
| - | [[Category: Lees, W | + | [[Category: Lees, W E.]] |
[[Category: Li, M.]] | [[Category: Li, M.]] | ||
| - | [[Category: Phylip, L | + | [[Category: Phylip, L H.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: proteinase a]] | [[Category: proteinase a]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:31 2008'' |
Revision as of 10:40, 21 February 2008
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STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21
Overview
The structures of the native Saccharomyces cerevisiae proteinase A have been solved by molecular replacement in the monoclinic and trigonal crystal forms and refined at 2.6-2.7A resolution. These structures agree overall with those of other uninhibited aspartic proteinases. However, an unusual orientation for the side chain of Tyr75, a conserved residue on the flexible "flap" that covers the active site and is important for the activity of these enzymes, was found in the trigonal crystals. A similar conformation of Tyr75 occupying the S1 substrate-binding pocket was previously reported only for chymosin (where it was interpreted as representing a "self-inhibited" state of the enzyme), but for no other aspartic proteinases. Since this orientation of Tyr75 has now been seen in the structures of two members of the family of aspartic proteinases, it might indicate that the placement of that residue in the S1 substrate-binding pocket might have some functional significance, analogous to what was seen for self-inhibited structures of serine proteinases.
About this Structure
1FMX is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Saccharopepsin, with EC number 3.4.23.25 Full crystallographic information is available from OCA.
Reference
An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae., Gustchina A, Li M, Phylip LH, Lees WE, Kay J, Wlodawer A, Biochem Biophys Res Commun. 2002 Jul 26;295(4):1020-6. PMID:12127998
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