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| - | [[Image:1uh4.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1uh4| PDB=1uh4 | SCENE= }} | | {{STRUCTURE_1uh4| PDB=1uh4 | SCENE= }} |
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| - | '''Thermoactinomyces vulgaris R-47 alpha-amylase 1/malto-tridecaose complex'''
| + | ===Thermoactinomyces vulgaris R-47 alpha-amylase 1/malto-tridecaose complex=== |
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| - | ==Overview==
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| - | The X-ray structures of complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) with an inhibitor acarbose and an inactive mutant TVAI with malto-hexaose and malto-tridecaose have been determined at 2.6, 2.0 and 1.8A resolution, and the structures have been refined to R-factors of 0.185 (R(free)=0.225), 0.184 (0.217) and 0.164 (0.200), respectively, with good chemical geometries. Acarbose binds to the catalytic site of TVAI, and interactions between acarbose and the enzyme are very similar to those found in other structure-solved alpha-amylase/acarbose complexes, supporting the proposed catalytic mechanism. Based on the structure of the TVAI/acarbose complex, the binding mode of pullulan containing alpha-(1,6) glucoside linkages could be deduced. Due to the structural difference caused by the replaced amino acid residue (Gln396 for Glu) in the catalytic site, malto-hexaose and malto-tridecaose partially bind to the catalytic site, giving a mimic of the enzyme/product complex. Besides the catalytic site, four sugar-binding sites on the molecular surface are found in these X-ray structures. Two sugar-binding sites in domain N hold the oligosaccharides with a regular helical structure of amylose, which suggests that the domain N is a starch-binding domain acting as an anchor to starch in the catalytic reaction of the enzyme. An assay of hydrolyzing activity for the raw starches confirmed that TVAI can efficiently hydrolyze raw starch. | + | The line below this paragraph, {{ABSTRACT_PUBMED_14687576}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14687576 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14687576}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tonozuka, T.]] | | [[Category: Tonozuka, T.]] |
| | [[Category: Starch binding domain]] | | [[Category: Starch binding domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:13:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:23:06 2008'' |
Revision as of 12:23, 27 July 2008
Template:STRUCTURE 1uh4
Thermoactinomyces vulgaris R-47 alpha-amylase 1/malto-tridecaose complex
Template:ABSTRACT PUBMED 14687576
About this Structure
1UH4 is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
Reference
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain., Abe A, Tonozuka T, Sakano Y, Kamitori S, J Mol Biol. 2004 Jan 16;335(3):811-22. PMID:14687576
Page seeded by OCA on Sun Jul 27 15:23:06 2008
