1uj4: Difference between revisions

Revision as of 13:31, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1uj4.png

Template:STRUCTURE 1uj4

Crystal structure of Thermus thermophilus ribose-5-phosphate isomeraseCrystal structure of Thermus thermophilus ribose-5-phosphate isomerase

Template:ABSTRACT PUBMED 13679361

About this StructureAbout this Structure

1UJ4 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi)., Hamada K, Ago H, Sugahara M, Nodake Y, Kuramitsu S, Miyano M, J Biol Chem. 2003 Dec 5;278(49):49183-90. Epub 2003 Sep 17. PMID:13679361

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase'''
+===Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase===
-==Overview==
+<!--
-Ribose-5-phosphate isomerase (Rpi) acts as a key enzyme in the oxidative and reductive pentose-phosphate pathways for the conversion of ribose-5-phosphate (R5P) to ribulose-5-phosphate and vice versa. We have determined the crystal structures of Rpi from Thermus thermophilus HB8 in complex with the open chain form of the substrate R5P and the open chain form of the C2 epimeric inhibitor arabinose-5-phosphate as well as the apo form at high resolution. The crystal structures of both complexes revealed that these ring-opened epimers are bound in the active site in a mirror symmetry binding mode. The O1 atoms are stabilized by an oxyanion hole composed of the backbone amide nitrogens in the conserved motif. In the structure of the Rpi.R5P complex, the conversion moiety O1-C1-C2-O2 in cis-configuration interacts with the carboxyl oxygens of Glu-108 in a water-excluded environment. Furthermore, the C2 hydroxyl group is presumed to be highly polarized by short hydrogen bonding with the side chain of Lys-99. R5P bound as the ring-opened reaction intermediate clarified the high stereoselectivity of the catalysis and is consistent with an aldose-ketose conversion by Rpi that proceeds via a cis-enediolate intermediate.
+The line below this paragraph, {{ABSTRACT_PUBMED_13679361}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 13679361 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_13679361}}
 ==About this Structure==
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 [[Category: Rsgi]]
 [[Category: Structural genomic]]
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