1gis
From Proteopedia
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| - | [[Image:1gis.gif|left|200px]] | + | [[Image:1gis.gif|left|200px]] |
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| - | '''A TRICHOSANTHIN(TCS) MUTANT(E85Q) COMPLEX STRUCTURE WITH 2'-DEOXY-ADENOSIN-5'-MONOPHOSPHATE''' | + | {{Structure |
| + | |PDB= 1gis |SIZE=350|CAPTION= <scene name='initialview01'>1gis</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''A TRICHOSANTHIN(TCS) MUTANT(E85Q) COMPLEX STRUCTURE WITH 2'-DEOXY-ADENOSIN-5'-MONOPHOSPHATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GIS is a [ | + | 1GIS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIS OCA]. |
==Reference== | ==Reference== | ||
| - | Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants., Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z, Protein Eng. 2003 Jun;16(6):391-6. PMID:[http:// | + | Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants., Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z, Protein Eng. 2003 Jun;16(6):391-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12874371 12874371] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichosanthes kirilowii]] | [[Category: Trichosanthes kirilowii]] | ||
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[[Category: DA]] | [[Category: DA]] | ||
[[Category: protein-sub complex]] | [[Category: protein-sub complex]] | ||
| - | [[Category: | + | [[Category: tc]] |
[[Category: trichosanthin]] | [[Category: trichosanthin]] | ||
| - | ''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 11:23:42 2008'' |
Revision as of 09:23, 20 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A TRICHOSANTHIN(TCS) MUTANT(E85Q) COMPLEX STRUCTURE WITH 2'-DEOXY-ADENOSIN-5'-MONOPHOSPHATE
Overview
Trichosanthin (TCS) is a type I ribosome-inactivating protein (RIP) which possesses rRNA N-glycosidase activity. In recent years, its immunomodulatory, anti-tumor and anti-HIV properties have been revealed. Here we report the crystal structures of several E85 mutant TCS complexes with adenosine-5'-monophosphate (AMP) and adenine. In E85Q TCS/AMP and E85A TCS/AMP, near the active site of the molecule and parallel to the aromatic ring of Tyr70, an AMP molecule is bound to the mutant without being hydrolyzed. In the E85R TCS/adenine complex, the hydrolyzed product adenine is located in the active pocket where it occupies a position similar to that in the TCS/NADPH complex. Significantly, AMP is bound in a position different to that of adenine. In comparison with these structures, we suggest that there are at least two subsites in the active site of TCS, one for initial substrate recognition as revealed by the AMP site and another for catalysis as represented by the NADPH site. Based on these complex structures, the function of residue 85 and the mechanism of catalysis are proposed.
About this Structure
1GIS is a Single protein structure of sequence from Trichosanthes kirilowii. Full crystallographic information is available from OCA.
Reference
Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants., Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z, Protein Eng. 2003 Jun;16(6):391-6. PMID:12874371
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