1mw3

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[[Image:1mw3.jpg|left|200px]]
[[Image:1mw3.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1mw3 |SIZE=350|CAPTION= <scene name='initialview01'>1mw3</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1mw3", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1mw3| PDB=1mw3 | SCENE= }}
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|RELATEDENTRY=[[1g5a|1G5A]], [[1jg9|1JG9]], [[1jgi|1JGI]], [[1mvy|1MVY]], [[1mw0|1MW0]], [[1mw1|1MW1]], [[1mw2|1MW2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mw3 OCA], [http://www.ebi.ac.uk/pdbsum/1mw3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mw3 RCSB]</span>
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}}
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'''Amylosucrase soaked with 1M sucrose'''
'''Amylosucrase soaked with 1M sucrose'''
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[[Category: Skov, L K.]]
[[Category: Skov, L K.]]
[[Category: Sprogoe, D.]]
[[Category: Sprogoe, D.]]
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[[Category: (beta-alpha)8 barrel]]
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[[Category: Protein-sugar complex]]
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[[Category: protein-sugar complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:47:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:55 2008''
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Revision as of 22:47, 2 May 2008

Template:STRUCTURE 1mw3

Amylosucrase soaked with 1M sucrose


Overview

The glucosyltransferase amylosucrase is structurally quite similar to the hydrolase alpha-amylase. How this switch in functionality is achieved is an important and fundamental question. The inactive E328Q amylosucrase variant has been co-crystallized with maltoheptaose, and the structure was determined by x-ray crystallography to 2.2 A resolution, revealing a maltoheptaose binding site in the B'-domain somewhat distant from the active site. Additional soaking of these crystals with maltoheptaose resulted in replacement of Tris in the active site with maltoheptaose, allowing the mapping of the -1 to +5 binding subsites. Crystals of amylosucrase were soaked with sucrose at different concentrations. The structures at approximately 2.1 A resolution revealed three new binding sites of different affinity. The highest affinity binding site is close to the active site but is not in the previously identified substrate access channel. Allosteric regulation seems necessary to facilitate access from this binding site. The structures show the pivotal role of the B'-domain in the transferase reaction. Based on these observations, an extension of the hydrolase reaction mechanism valid for this enzyme can be proposed. In this mechanism, the glycogen-like polymer is bound in the widest access channel to the active site. The polymer binding introduces structural changes that allow sucrose to migrate from its binding site into the active site and displace the polymer.

About this Structure

1MW3 is a Single protein structure of sequence from Neisseria polysaccharea. Full crystallographic information is available from OCA.

Reference

Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity., Skov LK, Mirza O, Sprogoe D, Dar I, Remaud-Simeon M, Albenne C, Monsan P, Gajhede M, J Biol Chem. 2002 Dec 6;277(49):47741-7. Epub 2002 Oct 2. PMID:12364331 Page seeded by OCA on Sat May 3 01:47:46 2008

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