1vah

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[[Image:1vah.gif|left|200px]]<br /><applet load="1vah" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vah.gif|left|200px]]
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caption="1vah, resolution 2.40&Aring;" />
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'''Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside'''<br />
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{{Structure
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|PDB= 1vah |SIZE=350|CAPTION= <scene name='initialview01'>1vah</scene>, resolution 2.40&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1VAH 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=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NPO:'>NPO</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=1VAH OCA].
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1VAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VAH OCA].
==Reference==
==Reference==
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Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site., Zhuo H, Payan F, Qian M, Protein J. 2004 Aug;23(6):379-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15517985 15517985]
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Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site., Zhuo H, Payan F, Qian M, Protein J. 2004 Aug;23(6):379-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15517985 15517985]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: CL]]
[[Category: CL]]
[[Category: NPO]]
[[Category: NPO]]
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[[Category: beta-alpha-barrels]]
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[[Category: beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:55 2008''

Revision as of 12:42, 20 March 2008

Image:1vah.gif


PDB ID 1vah

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: , and
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside


Overview

The X-ray structure analysis of a crystal of pig pancreatic alpha-amylase soaked with a rho-nitrophenyl-alpha-D-maltoside (pNPG2) substrate showed a pattern of electron density corresponding to the binding of a rho-nitrophenol unit at subsite -2 of the active site. Binding of the product to subsite -2 after hydrolysis of the pNPG2 molecules, may explain the low catalytic efficiency of the hydrolysis of pNPG2 by PPA. Except a small movement of the segment from residues 304-305 the typical conformational changes of the "flexible loop" (303-309), that constitutes the surface edge of the substrate binding cleft, were not observed in the present complex structure. This result supports the hypothesis that significant movement of the loop may depend on aglycone site being filled (Payan and Qian, J. Protein Chen. 22: 275, 2003). Structural analyses have shown that pancreatic alpha-amylases undergo an induced conformational change of the catalytic residue Asp300 upon substrate binding; in the present complex the catalytic residue is observed in its unliganded orientation. The results suggest that the induced reorientation is likely due to the presence of a sugar unit at subsite -1 and not linked to the closure of the flexible surface loop. The crystal structure was refined at 2.4 A resolution to an R factor of 17.55% (Rfree factor of 23.32%).

About this Structure

1VAH is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site., Zhuo H, Payan F, Qian M, Protein J. 2004 Aug;23(6):379-87. PMID:15517985

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