1M7H

Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer

Summary for 1M7H

• Entry DOI: 10.2210/pdb1m7h/pdb
• Related: 1D6J 1M7G
• Descriptor: Adenylylsulfate kinase, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: aps kinase, adenylylsulfate kinase, transferase, sulfate metabolism, nucleotide 2 kinase
• Biological source: Penicillium chrysogenum
• Total number of polymer chains: 4
• Total formula weight: 98935.25

Authors

Lansdon, E.B.,Sege, I.H.,Fisher, A.J. (deposition date: 2002-07-19, release date: 2002-11-27, Last modification date: 2024-04-03)

Primary citation

Lansdon, E.B.,Segel, I.H.,Fisher, A.J.
Ligand-Induced Structural Changes in Adenosine 5'-Phosphosulfate Kinase from Penicillium chrysogenum.
Biochemistry, 41:13672-13680, 2002

PubMed Abstract: 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.

PubMed: 12427029
DOI: 10.1021/bi026556b

Experimental method

X-RAY DIFFRACTION (2 Å)