1m7h: Difference between revisions

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[[Image:1m7h.jpg|left|200px]]<br /><applet load="1m7h" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1m7h.jpg|left|200px]]
caption="1m7h, resolution 2.00&Aring;" />
 
'''Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer'''<br />
{{Structure
|PDB= 1m7h |SIZE=350|CAPTION= <scene name='initialview01'>1m7h</scene>, resolution 2.00&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=ADX:ADENOSINE-5'-PHOSPHOSULFATE'>ADX</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25]
|GENE=
}}
 
'''Crystal Structure of APS kinase from Penicillium Chrysogenum: Structure with APS soaked out of one dimer'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1M7H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=ADX:'>ADX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7H OCA].  
1M7H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7H OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12427029 12427029]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12427029 12427029]
[[Category: Adenylyl-sulfate kinase]]
[[Category: Adenylyl-sulfate kinase]]
[[Category: Penicillium chrysogenum]]
[[Category: Penicillium chrysogenum]]
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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 13:39, 20 March 2008

File:1m7h.jpg


PDB ID 1m7h

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Activity: Adenylyl-sulfate kinase, with EC number 2.7.1.25
Coordinates: save as pdb, mmCIF, xml



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

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