2pbk

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[[Image:2pbk.jpg|left|200px]]<br /><applet load="2pbk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pbk.jpg|left|200px]]
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caption="2pbk, resolution 1.73&Aring;" />
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'''Crystal structure of KSHV protease in complex with hexapeptide phosphonate inhibitor'''<br />
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{{Structure
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|PDB= 2pbk |SIZE=350|CAPTION= <scene name='initialview01'>2pbk</scene>, resolution 1.73&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=GG7:'>GG7</scene>
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|ACTIVITY=
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|GENE= AF010430 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 Human herpesvirus 4])
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}}
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'''Crystal structure of KSHV protease in complex with hexapeptide phosphonate inhibitor'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=GG7:'>GG7</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBK OCA].
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2PBK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBK OCA].
==Reference==
==Reference==
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Substrate modulation of enzyme activity in the herpesvirus protease family., Lazic A, Goetz DH, Nomura AM, Marnett AB, Craik CS, J Mol Biol. 2007 Nov 2;373(4):913-23. Epub 2007 Aug 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17870089 17870089]
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Substrate modulation of enzyme activity in the herpesvirus protease family., Lazic A, Goetz DH, Nomura AM, Marnett AB, Craik CS, J Mol Biol. 2007 Nov 2;373(4):913-23. Epub 2007 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17870089 17870089]
[[Category: Human herpesvirus 4]]
[[Category: Human herpesvirus 4]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:11:12 2008''

Revision as of 16:11, 20 March 2008

Image:2pbk.jpg


PDB ID 2pbk

Drag the structure with the mouse to rotate
, resolution 1.73Å
Ligands: , and
Gene: AF010430 (Human herpesvirus 4)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of KSHV protease in complex with hexapeptide phosphonate inhibitor


Overview

The herpesvirus proteases are an example in which allosteric regulation of an enzyme activity is achieved through the formation of quaternary structure. Here, we report a 1.7 A resolution structure of Kaposi's sarcoma-associated herpesvirus protease in complex with a hexapeptide transition state analogue that stabilizes the dimeric state of the enzyme. Extended substrate binding sites are induced upon peptide binding. In particular, 104 A2 of surface are buried in the newly formed S4 pocket when tyrosine binds at this site. The peptide inhibitor also induces a rearrangement of residues that stabilizes the oxyanion hole and the dimer interface. Concomitant with the structural changes, an increase in catalytic efficiency of the enzyme results upon extended substrate binding. A nearly 20-fold increase in kcat/KM results upon extending the peptide substrate from a tetrapeptide to a hexapeptide exclusively due to a KM effect. This suggests that the mechanism by which herpesvirus proteases achieve their high specificity is by using extended substrates to modulate both the structure and activity of the enzyme.

About this Structure

2PBK is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.

Reference

Substrate modulation of enzyme activity in the herpesvirus protease family., Lazic A, Goetz DH, Nomura AM, Marnett AB, Craik CS, J Mol Biol. 2007 Nov 2;373(4):913-23. Epub 2007 Aug 16. PMID:17870089

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