1d6j

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[[Image:1d6j.jpg|left|200px]]
[[Image:1d6j.jpg|left|200px]]
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{{Structure
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|PDB= 1d6j |SIZE=350|CAPTION= <scene name='initialview01'>1d6j</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1d6j", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1d6j| PDB=1d6j | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6j OCA], [http://www.ebi.ac.uk/pdbsum/1d6j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6j RCSB]</span>
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'''CRYSTAL STRUCTURE OF ADENOSINE 5'-PHOSPHOSULFATE (APS) KINASE FROM PENICILLIUM CHRYSOGENUM'''
'''CRYSTAL STRUCTURE OF ADENOSINE 5'-PHOSPHOSULFATE (APS) KINASE FROM PENICILLIUM CHRYSOGENUM'''
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[[Category: MacRae, I J.]]
[[Category: MacRae, I J.]]
[[Category: Segel, I H.]]
[[Category: Segel, I H.]]
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[[Category: adenylylsulfate kinase]]
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[[Category: Adenylylsulfate kinase]]
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[[Category: aps kinase]]
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[[Category: Aps kinase]]
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[[Category: nucleotide kinase]]
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[[Category: Nucleotide kinase]]
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[[Category: sulfate]]
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[[Category: Sulfate]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:30:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:45 2008''
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Revision as of 10:30, 2 May 2008

Template:STRUCTURE 1d6j

CRYSTAL STRUCTURE OF ADENOSINE 5'-PHOSPHOSULFATE (APS) KINASE FROM PENICILLIUM CHRYSOGENUM


Overview

Adenosine 5'-phosphosulfate (APS) kinase catalyzes the second reaction in the two-step conversion of inorganic sulfate to 3'-phosphoadenosine 5'-phosphosulfate (PAPS). This report presents the 2.0 A resolution crystal structure of ligand-free APS kinase from the filamentous fungus, Penicillium chrysogenum. The enzyme crystallized as a homodimer with each subunit folded into a classic kinase motif consisting of a twisted, parallel beta-sheet sandwiched between two alpha-helical bundles. The Walker A motif, (32)GLSASGKS(39), formed the predicted P-loop structure. Superposition of the APS kinase active site region onto several other P-loop-containing proteins revealed that the conserved aspartate residue that usually interacts with the Mg(2+) coordination sphere of MgATP is absent in APS kinase. However, upon MgATP binding, a different aspartate, Asp 61, could shift and bind to the Mg(2+). The sequence (156)KAREGVIKEFT(166), which has been suggested to be a (P)APS motif, is located in a highly protease-susceptible loop that is disordered in both subunits of the free enzyme. MgATP or MgADP protects against proteolysis; APS alone has no effect but augments the protection provided by MgADP. The results suggest that the loop lacks a fixed structure until MgATP or MgADP is bound. The subsequent conformational change together with the potential change promoted by the interaction of MgATP with Asp 61 may define the APS binding site. This model is consistent with the obligatory ordered substrate binding sequence (MgATP or MgADP before APS) as established from steady state kinetics and equilibrium binding studies.

About this Structure

1D6J is a Single protein structure of sequence from Penicillium chrysogenum. Full crystallographic information is available from OCA.

Reference

Crystal structure of adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum., MacRae IJ, Segel IH, Fisher AJ, Biochemistry. 2000 Feb 22;39(7):1613-21. PMID:10677210 Page seeded by OCA on Fri May 2 13:30:22 2008

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