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1uqu

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[[Image:1uqu.gif|left|200px]]
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{{STRUCTURE_1uqu| PDB=1uqu | SCENE= }}
{{STRUCTURE_1uqu| PDB=1uqu | SCENE= }}
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'''TREHALOSE-6-PHOSPHATE FROM E. COLI BOUND WITH UDP-GLUCOSE.'''
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===TREHALOSE-6-PHOSPHATE FROM E. COLI BOUND WITH UDP-GLUCOSE.===
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==Overview==
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Trehalose is an unusual non-reducing disaccharide that plays a variety of biological roles, from food storage to cellular protection from environmental stresses such as desiccation, pressure, heat-shock, extreme cold, and oxygen radicals. It is also an integral component of the cell-wall glycolipids of mycobacteria. The primary enzymatic route to trehalose first involves the transfer of glucose from a UDP-glucose donor to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. This reaction, in which the configurations of two glycosidic bonds are set simultaneously, is catalyzed by the glycosyltransferase trehalose-6-phosphate synthase (OtsA), which acts with retention of the anomeric configuration of the UDP-sugar donor. The classification of activated sugar-dependent glycosyltransferases into approximately 70 distinct families based upon amino acid sequence similarities places OtsA in glycosyltransferase family 20 (see afmb.cnrs-mrs.fr/CAZY/). The recent 2.4 A structure of Escherichia coli OtsA revealed a two-domain enzyme with catalysis occurring at the interface of the twin beta/alpha/beta domains. Here we present the 2.0 A structures of the E. coli OtsA in complex with either UDP-Glc or the non-transferable analogue UDP-2-deoxy-2-fluoroglucose. Both complexes unveil the donor subsite interactions, confirming a strong similarity to glycogen phosphorylases, and reveal substantial conformational differences to the previously reported complex with UDP and glucose 6-phosphate. Both the relative orientation of the two domains and substantial (up to 10 A) movements of an N-terminal loop (residues 9-22) characterize the more open "relaxed" conformation of the binary UDP-sugar complexes reported here.
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(as it appears on PubMed at http://www.pubmed.gov), where 14570926 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14570926}}
==About this Structure==
==About this Structure==
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[[Category: Synthase]]
[[Category: Synthase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:33:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:47:36 2008''

Revision as of 11:47, 27 July 2008

Image:1uqu.png

Template:STRUCTURE 1uqu

TREHALOSE-6-PHOSPHATE FROM E. COLI BOUND WITH UDP-GLUCOSE.

Template:ABSTRACT PUBMED 14570926

About this Structure

1UQU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution., Gibson RP, Tarling CA, Roberts S, Withers SG, Davies GJ, J Biol Chem. 2004 Jan 16;279(3):1950-5. Epub 2003 Oct 21. PMID:14570926

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