This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1uj5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uj5.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1uj5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uj5| PDB=1uj5 | SCENE= }}
{{STRUCTURE_1uj5| PDB=1uj5 | SCENE= }}
-
'''Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase complexed with ribose-5-phosphate'''
+
===Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase complexed with ribose-5-phosphate===
-
==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.
 +
-->
 +
{{ABSTRACT_PUBMED_13679361}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:18:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:29:07 2008''

Revision as of 21:29, 28 July 2008

Image:1uj5.png

Template:STRUCTURE 1uj5

Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase complexed with ribose-5-phosphate

Template:ABSTRACT PUBMED 13679361

About this Structure

1UJ5 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 29 00:29:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uj5"
Personal tools