1oio: Difference between revisions
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[[Image:1oio.jpg|left|200px]]<br /><applet load="1oio" size=" | [[Image:1oio.jpg|left|200px]]<br /><applet load="1oio" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oio, resolution 1.70Å" /> | caption="1oio, resolution 1.70Å" /> | ||
'''GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI'''<br /> | '''GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Nag Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 1OIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: n-acetyl-d-glucosamine binding]] | [[Category: n-acetyl-d-glucosamine binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:58:36 2008'' | ||
Revision as of 10:58, 3 February 2008
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GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI
OverviewOverview
GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal, disease, and the structure of the ligand-binding domain, GafD1-178, has, been determined at 1.7A resolution in the presence of the receptor sugar, N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold., The ligand-binding site was identified and localized to the side of the, molecule. Receptor binding is mediated by side-chain as well main-chain, interactions. Ala43-Asn44, Ser116-Thr117 form the sugar acetamide, specificity pocket, while Asp88 confers tight binding and Trp109 appears, to position the ligand. There is a disulfide bond that rigidifies the, acetamide specificity pocket. The three fimbrial lectins, GafD, FimH and, PapG share similar beta-barrel folds but display different ligand-binding, regions and disulfide-bond patterns. We suggest an evolutionary path for, the evolution of the very diverse fimbrial lectins from a common ancestral, fold.
About this StructureAbout this Structure
1OIO is a Single protein structure of sequence from Escherichia coli with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia., Merckel MC, Tanskanen J, Edelman S, Westerlund-Wikstrom B, Korhonen TK, Goldman A, J Mol Biol. 2003 Aug 22;331(4):897-905. PMID:12909017
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