1yth

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[[Image:1yth.jpg|left|200px]]<br /><applet load="1yth" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yth.jpg|left|200px]]
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caption="1yth, resolution 2.2&Aring;" />
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'''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''<br />
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{{Structure
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|PDB= 1yth |SIZE=350|CAPTION= <scene name='initialview01'>1yth</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|ACTIVITY= [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]
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|GENE= STRAIN SF-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1YTH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTH OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8841139 8841139]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8841139 8841139]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: HIV-1 retropepsin]]
[[Category: HIV-1 retropepsin]]
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[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: ) aids]]
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[[Category: ) aid]]
[[Category: aspartyl protease]]
[[Category: aspartyl protease]]
[[Category: complex (hydrolase/peptide]]
[[Category: complex (hydrolase/peptide]]
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[[Category: rna-directed dna polymerase]]
[[Category: rna-directed dna polymerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:27:20 2008''

Revision as of 13:27, 20 March 2008


PDB ID 1yth

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands:
Gene: STRAIN SF-2 (Escherichia coli)
Activity: HIV-1 retropepsin, with EC number 3.4.23.16
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 15:27:20 2008

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