1wkr
From Proteopedia
(New page: 200px<br /><applet load="1wkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkr, resolution 1.30Å" /> '''Crystal structure of...) |
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| - | [[Image:1wkr.gif|left|200px]]<br /><applet load="1wkr" size=" | + | [[Image:1wkr.gif|left|200px]]<br /><applet load="1wkr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wkr, resolution 1.30Å" /> | caption="1wkr, resolution 1.30Å" /> | ||
'''Crystal structure of aspartic proteinase from Irpex lacteus'''<br /> | '''Crystal structure of aspartic proteinase from Irpex lacteus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in | + | The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in complex with pepstatin (a six amino acid residue peptide-like inhibitor) was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely distributed in nature, with high milk-clotting activity relative to proteolytic activity. The overall structure was in good topological agreement with pepsin and other aspartic proteases. The structure and interaction pattern around the catalytic site were conserved, in agreement with the other aspartic proteinase/inhibitor complex structures reported previously. The high-resolution data also supported the transition state model, as proposed previously for the catalytic mechanism of aspartic proteinase. Unlike the other aspartic proteinases, ILAP was found to require hydrophobic residues either in the P(1) or P(1') site, and also in the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor complex structure also revealed the substrate binding mechanism of ILAP at the P(3) and P(4) site of the substrate, where the inserted loop built up the unique hydrophobic pocket at the P(4) site. |
==About this Structure== | ==About this Structure== | ||
| - | 1WKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Irpex_lacteus Irpex lacteus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polyporopepsin Polyporopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.29 3.4.23.29] Full crystallographic information is available from [http:// | + | 1WKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Irpex_lacteus Irpex lacteus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polyporopepsin Polyporopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.29 3.4.23.29] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: enzyme-inhibitor complex]] | [[Category: enzyme-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:32 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal structure of aspartic proteinase from Irpex lacteus
Overview
The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in complex with pepstatin (a six amino acid residue peptide-like inhibitor) was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely distributed in nature, with high milk-clotting activity relative to proteolytic activity. The overall structure was in good topological agreement with pepsin and other aspartic proteases. The structure and interaction pattern around the catalytic site were conserved, in agreement with the other aspartic proteinase/inhibitor complex structures reported previously. The high-resolution data also supported the transition state model, as proposed previously for the catalytic mechanism of aspartic proteinase. Unlike the other aspartic proteinases, ILAP was found to require hydrophobic residues either in the P(1) or P(1') site, and also in the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor complex structure also revealed the substrate binding mechanism of ILAP at the P(3) and P(4) site of the substrate, where the inserted loop built up the unique hydrophobic pocket at the P(4) site.
About this Structure
1WKR is a Single protein structure of sequence from Irpex lacteus with as ligand. Active as Polyporopepsin, with EC number 3.4.23.29 Full crystallographic information is available from OCA.
Reference
Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin., Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H, J Mol Biol. 2004 Aug 27;341(5):1227-35. PMID:15321718
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