1d6j
From Proteopedia
(New page: 200px<br /><applet load="1d6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d6j, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1d6j.jpg|left|200px]]<br /><applet load="1d6j" size=" | + | [[Image:1d6j.jpg|left|200px]]<br /><applet load="1d6j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d6j, resolution 2.00Å" /> | caption="1d6j, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF ADENOSINE 5'-PHOSPHOSULFATE (APS) KINASE FROM PENICILLIUM CHRYSOGENUM'''<br /> | '''CRYSTAL STRUCTURE OF ADENOSINE 5'-PHOSPHOSULFATE (APS) KINASE FROM PENICILLIUM CHRYSOGENUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adenosine 5'-phosphosulfate (APS) kinase catalyzes the second reaction in | + | 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== | ==About this Structure== | ||
| - | 1D6J 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 TLA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1D6J 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=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1D6J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Penicillium chrysogenum]] | [[Category: Penicillium chrysogenum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fisher, A | + | [[Category: Fisher, A J.]] |
| - | [[Category: MacRae, I | + | [[Category: MacRae, I J.]] |
| - | [[Category: Segel, I | + | [[Category: Segel, I H.]] |
[[Category: TLA]] | [[Category: TLA]] | ||
[[Category: adenylylsulfate kinase]] | [[Category: adenylylsulfate kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:30 2008'' |
Revision as of 10:13, 21 February 2008
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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 with as ligand. Active as Adenylyl-sulfate kinase, with EC number 2.7.1.25 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
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