5apr: Difference between revisions

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STRUCTURES OF COMPLEXES OF RHIZOPUSPEPSIN WITH PEPSTATIN AND OTHER STATINE-CONTAINING INHIBITORS

OverviewOverview

The three-dimensional structures of the complexes of the aspartic proteinase from Rhizopus chinensis (Rhizopuspepsin, EC 3.4.23.6) with pepstatin and two pepstatin-like peptide inhibitors of renin have been determined by X-ray diffraction methods and refined by restrained least-squares procedures. The inhibitors adopt an extended conformation and lie in the deep groove located between the two domains of the enzyme. Inhibitor binding is accompanied by a conformational change at the "flap," a beta-hairpin loop region, that projects over the binding cleft and closes down over the inhibitor, excluding water molecules from the vicinity of the scissile bond. The hydroxyl group of the central statyl residue of the inhibitors replaces the water molecule found between the two active aspartates, Asp-35 and Asp-218, in the native structure. The refined structures provide additional data to define the specific subsites of the enzyme and also show a system of hydrogen bonding to the inhibitor backbone similar to that observed for a reduced inhibitor.

About this StructureAbout this Structure

5APR is a Single protein structure of sequence from [1] with as ligand. Active as Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 Full crystallographic information is available from OCA.

ReferenceReference

Structures of complexes of rhizopuspepsin with pepstatin and other statine-containing inhibitors., Suguna K, Padlan EA, Bott R, Boger J, Parris KD, Davies DR, Proteins. 1992 Jul;13(3):195-205. PMID:1603809

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OCA

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-[[Image:5apr.gif|left|200px]]<br /><applet load="5apr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:5apr.gif|left|200px]]<br /><applet load="5apr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="5apr, resolution 2.1&Aring;" />
 '''STRUCTURES OF COMPLEXES OF RHIZOPUSPEPSIN WITH PEPSTATIN AND OTHER STATINE-CONTAINING INHIBITORS'''<br />
 ==Overview==
-The three-dimensional structures of the complexes of the aspartic, proteinase from Rhizopus chinensis (Rhizopuspepsin, EC 3.4.23.6) with, pepstatin and two pepstatin-like peptide inhibitors of renin have been, determined by X-ray diffraction methods and refined by restrained, least-squares procedures. The inhibitors adopt an extended conformation, and lie in the deep groove located between the two domains of the enzyme., Inhibitor binding is accompanied by a conformational change at the "flap,", a beta-hairpin loop region, that projects over the binding cleft and, closes down over the inhibitor, excluding water molecules from the, vicinity of the scissile bond. The hydroxyl group of the central statyl, residue of the inhibitors replaces the water molecule found between the, two active aspartates, Asp-35 and Asp-218, in the native structure. The, refined structures provide additional data to define the specific subsites, of the enzyme and also show a system of hydrogen bonding to the inhibitor, backbone similar to that observed for a reduced inhibitor.
+The three-dimensional structures of the complexes of the aspartic proteinase from Rhizopus chinensis (Rhizopuspepsin, EC 3.4.23.6) with pepstatin and two pepstatin-like peptide inhibitors of renin have been determined by X-ray diffraction methods and refined by restrained least-squares procedures. The inhibitors adopt an extended conformation and lie in the deep groove located between the two domains of the enzyme. Inhibitor binding is accompanied by a conformational change at the "flap," a beta-hairpin loop region, that projects over the binding cleft and closes down over the inhibitor, excluding water molecules from the vicinity of the scissile bond. The hydroxyl group of the central statyl residue of the inhibitors replaces the water molecule found between the two active aspartates, Asp-35 and Asp-218, in the native structure. The refined structures provide additional data to define the specific subsites of the enzyme and also show a system of hydrogen bonding to the inhibitor backbone similar to that observed for a reduced inhibitor.
 ==About this Structure==
-APR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5APR OCA].
+APR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5APR OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Hydrolase]]
 [[Category: Single protein]]
-[[Category: Davies, D.R.]]
+[[Category: Davies, D R.]]
 [[Category: Suguna, K.]]
 [[Category: CA]]
 [[Category: hydrolase (acid proteinase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:24:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:50 2008''