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-[[Image:1xtz.gif|left|200px]]
+{{Seed}}
+[[Image:1xtz.png|left|200px]]
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 {{STRUCTURE_1xtz|  PDB=1xtz  |  SCENE=  }}
-'''Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes'''
+===Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes===
-==Overview==
+<!--
-Ribose-5-phosphate isomerase A has an important role in sugar metabolism by interconverting ribose-5-phosphate and ribulose-5-phosphate. This enzyme is ubiquitous and highly conserved among the three kingdoms of life. We have solved the 2.1 A resolution crystal structure of the Saccharomyces cerevisiae enzyme by molecular replacement. This protein adopts the same fold as its archaeal and bacterial orthologs with two alpha/beta domains tightly packed together. Mapping of conserved residues at the surface of the protein reveals strong invariability of the active site pocket, suggesting a common ligand binding mode and a similar catalytic mechanism. The yeast enzyme associates as a homotetramer similarly to the archaeal protein. The effect of an inactivating mutation (Arg189 to Lys) is discussed in view of the information brought by this structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_16054529}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16054529 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16054529}}
 ==About this Structure==
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 [[Category: D-ribose-5-phosphate isomerase]]
 [[Category: Yeast]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:30:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:47:34 2008''