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'''Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer''' | '''Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer''' | ||
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[[Category: Lansdon, E B.]] | [[Category: Lansdon, E B.]] | ||
[[Category: Sege, I H.]] | [[Category: Sege, I H.]] | ||
[[Category: | [[Category: Adenylylsulfate kinase]] | ||
[[Category: | [[Category: Aps kinase]] | ||
[[Category: | [[Category: Nucleotide 2 kinase]] | ||
[[Category: | [[Category: Sulfate metabolism]] | ||
[[Category: | [[Category: Transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:43:43 2008'' | |||
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Revision as of 00:43, 3 May 2008
Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer
OverviewOverview
Adenosine 5'-phosphosulfate (APS) kinase catalyzes the second reaction in the two-step, ATP-dependent conversion of inorganic sulfate to 3'-phosphoadenosine 5'-phosphosulfate (PAPS). PAPS serves as the sulfuryl donor for the biosynthesis of all sulfate esters and also as a precursor of reduced sulfur biomolecules in many organisms. Previously, we determined the crystal structure of ligand-free APS kinase from the filamentous fungus, Penicillium chrysogenum [MacRae et al. (2000) Biochemistry 39, 1613-1621]. That structure contained a protease-susceptible disordered region ("mobile lid"; residues 145-170). Addition of MgADP and APS, which together promote the formation of a nonproductive "dead-end" ternary complex, protected the lid from trypsin. This report presents the 1.43 A resolution crystal structure of APS kinase with both ADP and APS bound at the active site and the 2.0 A resolution structure of the enzyme with ADP alone bound. The mobile lid is ordered in both complexes and is shown to provide part of the binding site for APS. That site is formed primarily by the highly conserved Arg 66, Arg 80, and Phe 75 from the protein core and Phe 165 from the mobile lid. The two Phe residues straddle the adenine ring of bound APS. Arg 148, a completely conserved residue, is the only residue in the mobile lid that interacts directly with bound ADP. Ser 34, located in the apex of the P-loop, hydrogen-bonds to the 3'-OH of APS, the phosphoryl transfer target. The structure of the binary E.ADP complex revealed further changes in the active site and N-terminal helix that occur upon the binding/release of (P)APS.
About this StructureAbout this Structure
1M7H is a Single protein structure of sequence from Penicillium chrysogenum. Full crystallographic information is available from OCA.
ReferenceReference
Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum., Lansdon EB, Segel IH, Fisher AJ, Biochemistry. 2002 Nov 19;41(46):13672-80. PMID:12427029 Page seeded by OCA on Sat May 3 00:43:43 2008