1yth
From Proteopedia
(New page: 200px<br /> <applet load="1yth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yth, resolution 2.2Å" /> '''SIV PROTEASE CRYSTAL...) |
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| - | [[Image:1yth. | + | [[Image:1yth.jpg|left|200px]]<br /><applet load="1yth" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1yth, resolution 2.2Å" /> | caption="1yth, resolution 2.2Å" /> | ||
'''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''<br /> | '''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http:// | + | 1YTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna-directed dna polymerase]] | [[Category: rna-directed dna polymerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:12:41 2008'' |
Revision as of 15:12, 15 February 2008
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SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT
Overview
Strain is eliminated as a factor in hydrolysis of the scissile peptide, bond by human immunodeficiency virus (HIV)-1 and simian immunodeficiency, virus (SIV), based on the first eight complexes of products of hydrolysis, with the enzymes. The carboxyl group generated at the scissile bond, interacts with both catalytic aspartic acids. The structures directly, suggest the interactions of the gemdiol intermediate with the active site., Based on the structures, the nucleophilic water is displaced, stereospecifically by substrate binding toward one catalytic aspartic, acid, while the scissile carbonyl becomes hydrogen bonded to the other, catalytic aspartic acid in position for hydrolysis. Crystal structures for, two N-terminal (P) products and two C-terminal (Q) products provide, unambiguous density for the ligands at 2.2-2.6 A resolution and 17-21% R, factors. The N-terminal product, Ac-S-L-N-F/, overlaps closely with the, N-terminal sequences of peptidomimetic inhibitors bound to the protease., Comparison of the two C-terminal products, /F-L-E-K and /F(NO2)-E-A-Nle-S, indicates that the P2' residue is highly constrained, while the, positioning of the P1' and P3' residues are sequence dependent.
About this Structure
1YTH is a Single protein structure of sequence from Escherichia coli with as ligand. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.
Reference
Three-dimensional structures of HIV-1 and SIV protease product complexes., Rose RB, Craik CS, Douglas NL, Stroud RM, Biochemistry. 1996 Oct 1;35(39):12933-44. PMID:8841139
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