1ylh: Difference between revisions

Revision as of 19:45, 27 July 2008

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File:1ylh.png

Template:STRUCTURE 1ylh

Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and PyruvateCrystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate

Template:ABSTRACT PUBMED 15983413

About this StructureAbout this Structure

1YLH is a Single protein structure of sequence from Actinobacillus succinogenes. Full crystallographic information is available from OCA.

ReferenceReference

Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif., Leduc YA, Prasad L, Laivenieks M, Zeikus JG, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):903-12. Epub 2005, Jun 24. PMID:15983413

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OCA

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 {{STRUCTURE_1ylh|  PDB=1ylh  |  SCENE=  }}
-'''Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate'''
+===Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate===
-==Overview==
+<!--
-Actinobacillus succinogenes can produce, via fermentation, high concentrations of succinate, an important industrial commodity. A key enzyme in this pathway is phosphoenolpyruvate carboxykinase (PCK), which catalyzes the production of oxaloacetate from phosphoenolpyruvate and carbon dioxide, with the concomitant conversion of adenosine 5'-diphosphate to adenosine 5'-triphosphate. 1.85 and 1.70 A resolution structures of the native and a pyruvate/Mn(2+)/phosphate complex have been solved, respectively. The structure of the complex contains sulfhydryl reducing agents covalently bound to three cysteine residues via disulfide bonds. One of these cysteine residues (Cys285) is located in the active-site cleft and may be analogous to the putative reactive cysteine of PCK from Trypanosoma cruzi. Cys285 is also part of a previously unreported conserved motif comprising residues 280-287 and containing the pattern NXEXGXY(/F)A(/G); this new motif appears to have a structural role in stabilizing and positioning side chains that bind substrates and metal ions. The first few residues of this motif connect the two domains of the enzyme and a fulcrum point appears to be located near Asn280. In addition, an active-site Asp residue forms two coordinate bonds with the Mn(2+) ion present in the structure of the complex in a symmetrical bidentate manner, unlike in other PCK structures that contain a manganese ion.
+The line below this paragraph, {{ABSTRACT_PUBMED_15983413}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15983413 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15983413}}
 ==About this Structure==
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 [[Category: Disulphide bond]]
 [[Category: Phosphoenolpyruvate carboxykinase]]
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