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3amk
From Proteopedia
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| - | [[ | + | ==Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L== |
| + | <StructureSection load='3amk' size='340' side='right' caption='[[3amk]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3amk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryza_sativa_japonica_group Oryza sativa japonica group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AMK FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Os06g0726400, SBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Oryza sativa Japonica Group])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3amk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3amk RCSB], [http://www.ebi.ac.uk/pdbsum/3amk PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Starch-branching enzyme catalyzes the cleavage of alpha-1, 4-linkages and the subsequent transfer of alpha-1,4 glucan to form an alpha-1,6 branch point in amylopectin. Sequence analysis of the rice-branching enzyme I (BEI) indicated a modular structure in which the central alpha-amylase domain is flanked on each side by the N-terminal carbohydrate-binding module 48 and the alpha-amylase C-domain. We determined the crystal structure of BEI at a resolution of 1.9 A by molecular replacement using the Escherichia coli glycogen BE as a search model. Despite three modular structures, BEI is roughly ellipsoidal in shape with two globular domains that form a prominent groove which is proposed to serve as the alpha-polyglucan-binding site. Amino acid residues Asp344 and Glu399, which are postulated to play an essential role in catalysis as a nucleophile and a general acid/base, respectively, are located at a central cleft in the groove. Moreover, structural comparison revealed that in BEI, extended loop structures cause a narrowing of the substrate-binding site, whereas shortened loop structures make a larger space at the corresponding subsite in the Klebsiella pneumoniae pullulanase. This structural difference might be attributed to distinct catalytic reactions, transglycosylation and hydrolysis, respectively, by BEI and pullulanase. | ||
| - | + | Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding.,Noguchi J, Chaen K, Vu NT, Akasaka T, Shimada H, Nakashima T, Nishi A, Satoh H, Omori T, Kakuta Y, Kimura M Glycobiology. 2011 Aug;21(8):1108-16. Epub 2011 Apr 14. PMID:21493662<ref>PMID:21493662</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
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[[Category: Oryza sativa japonica group]] | [[Category: Oryza sativa japonica group]] | ||
[[Category: Chaen, K.]] | [[Category: Chaen, K.]] | ||
Revision as of 11:05, 14 May 2014
Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L
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