1ua3

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(New page: 200px<br /><applet load="1ua3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ua3, resolution 2.01&Aring;" /> '''Crystal structure of...)
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caption="1ua3, resolution 2.01&Aring;" />
caption="1ua3, resolution 2.01&Aring;" />
'''Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides'''<br />
'''Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides'''<br />
==Overview==
==Overview==
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The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked, (and flash-frozen) with a maltopentaose substrate showed a pattern of, electron density corresponding to the binding of oligosaccharides at the, active site and at three surface binding sites. The electron density, region observed at the active site, filling subsites-3 through-1, was, interpreted in terms of the process of enzyme-catalyzed hydrolysis, undergone by maltopentaose. Because the expected conformational changes in, the "flexible loop" that constitutes the surface edge of the active site, were not observed, the movement of the loop may depend on aglycone site, being filled. The crystal structure was refined at 2.01 A resolution to an, R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of, 3910 protein atoms, one calcium ion, two chloride ions, 103, oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene, glycol atoms.
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The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms.
==About this Structure==
==About this Structure==
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1UA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with GLC, MAL, CL, CA, MLR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UA3 OCA].
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1UA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MLR:'>MLR</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA3 OCA].
==Reference==
==Reference==
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[[Category: beta-alpha-barrels]]
[[Category: beta-alpha-barrels]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:57:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:15 2008''

Revision as of 13:22, 21 February 2008

Image:1ua3.jpg

1ua3, resolution 2.01Å

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Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

Overview

The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms.

About this Structure

1UA3 is a Single protein structure of sequence from Sus scrofa with , , , , and as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides., Payan F, Qian M, J Protein Chem. 2003 Apr;22(3):275-84. PMID:12962327

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