1oxm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1oxm.jpg|left|200px]] | [[Image:1oxm.jpg|left|200px]] | ||
'''STRUCTURE OF CUTINASE''' | {{Structure | ||
|PDB= 1oxm |SIZE=350|CAPTION= <scene name='initialview01'>1oxm</scene>, resolution 2.30Å | |||
|SITE= <scene name='pdbsite=TC4:Catalytic+Triad'>TC4</scene> | |||
|LIGAND= <scene name='pdbligand=TC4:BUTYL-PHOSPHINIC ACID 2,3-BIS-BUTYLCARBAMOYLOXY-PROPYL ESTER GROUP'>TC4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF CUTINASE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1OXM is a [ | 1OXM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXM OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of cutinase covalently inhibited by a triglyceride analogue., Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C, Protein Sci. 1997 Feb;6(2):275-86. PMID:[http:// | Crystal structure of cutinase covalently inhibited by a triglyceride analogue., Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C, Protein Sci. 1997 Feb;6(2):275-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9041628 9041628] | ||
[[Category: Fusarium solani subsp. pisi]] | [[Category: Fusarium solani subsp. pisi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: serine esterase]] | [[Category: serine esterase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:17:02 2008'' | ||
Revision as of 14:17, 20 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF CUTINASE
OverviewOverview
Cutinase from Fusarium solani is a lipolytic enzyme that hydrolyses triglycerides efficiently. All the inhibited forms of lipolytic enzymes described so far are based on the use of small organophosphate and organophosphonate inhibitors, which bear little resemblance to a natural triglyceride substrate. In this article we describe the crystal structure of cutinase covalently inhibited by (R)-1,2-dibutyl-carbamoylglycero-3-O-p-nitrophenylbutyl-phos phonate, a triglyceride analogue mimicking the first tetrahedral intermediate along the reaction pathway. The structure, which has been solved at 2.3 A, reveals that in both the protein molecules of the asymmetric unit the inhibitor is almost completely embedded in the active site crevice. The overall shape of the inhibitor is that of a fork: the two dibutyl-carbamoyl chains point towards the surface of the protein, whereas the butyl chain bound to the phosphorous atom is roughly perpendicular to the sn-1 and sn-2 chains. The sn-3 chain is accommodated in a rather small pocket at the bottom of the active site crevice, thus providing a structural explanation for the preference of cutinase for short acyl chain substrates.
About this StructureAbout this Structure
1OXM is a Single protein structure of sequence from Fusarium solani subsp. pisi. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cutinase covalently inhibited by a triglyceride analogue., Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C, Protein Sci. 1997 Feb;6(2):275-86. PMID:9041628
Page seeded by OCA on Thu Mar 20 13:17:02 2008