1sd0

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[[Image:1sd0.jpg|left|200px]]<br /><applet load="1sd0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sd0.jpg|left|200px]]
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caption="1sd0, resolution 2.3&Aring;" />
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'''Structure of arginine kinase C271A mutant'''<br />
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{{Structure
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|PDB= 1sd0 |SIZE=350|CAPTION= <scene name='initialview01'>1sd0</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3]
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|GENE= ak ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6850 Limulus polyphemus])
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}}
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'''Structure of arginine kinase C271A mutant'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus] with <scene name='pdbligand=NO3:'>NO3</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ARG:'>ARG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD0 OCA].
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1SD0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD0 OCA].
==Reference==
==Reference==
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The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants., Gattis JL, Ruben E, Fenley MO, Ellington WR, Chapman MS, Biochemistry. 2004 Jul 13;43(27):8680-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15236576 15236576]
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The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants., Gattis JL, Ruben E, Fenley MO, Ellington WR, Chapman MS, Biochemistry. 2004 Jul 13;43(27):8680-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15236576 15236576]
[[Category: Arginine kinase]]
[[Category: Arginine kinase]]
[[Category: Limulus polyphemus]]
[[Category: Limulus polyphemus]]
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[[Category: transition state]]
[[Category: transition state]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:03:24 2008''

Revision as of 12:03, 20 March 2008

Image:1sd0.jpg


PDB ID 1sd0

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , , , and
Gene: ak (Limulus polyphemus)
Activity: Arginine kinase, with EC number 2.7.3.3
Coordinates: save as pdb, mmCIF, xml



Structure of arginine kinase C271A mutant


Overview

Arginine kinase buffers cellular ATP levels by catalyzing reversible phosphoryl transfer between ATP and arginine. A conserved cysteine has long been thought important in catalysis. Here, cysteine 271 of horseshoe crab arginine kinase has been mutated to serine, alanine, asparagine, or aspartate. Catalytic turnover rates were 0.02-1.0% of wild type, but the activity of uncharged mutations could be partially rescued with chloride. Steady-state binding constants were slightly increased, more so for phospho-L-arginine than ADP. Substrate binding synergy observed in many phosphagen kinases was reduced or eliminated in mutant enzymes. The crystallographic structure of the alanine mutant at 2.3 A resolution, determined as a transition state analogue complex with arginine, nitrate, and MgADP, was nearly identical to wild type. Enzyme-substrate interactions are maintained as in wild type, and substrates remain at least roughly aligned for in-line phosphoryl transfer. Homology models with serine, asparagine, or aspartate replacing the active site cysteine similarly show only minor structural changes. Most striking, however, is the presence in the C271A mutant crystallographic structure of a chloride ion within 3.5 A of the nonreactive N(eta) substrate nitrogen, approximating the position of the sulfur in the wild-type's cysteine. Together, the results contradict prevailing speculation that the cysteine mediates a substrate-induced conformational change, confirm that it is the thiolate form that is relevant to catalysis, and suggest that one of its roles is to help to enhance the catalytic rate through electrostatic stabilization of the transition state.

About this Structure

1SD0 is a Single protein structure of sequence from Limulus polyphemus. Full crystallographic information is available from OCA.

Reference

The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants., Gattis JL, Ruben E, Fenley MO, Ellington WR, Chapman MS, Biochemistry. 2004 Jul 13;43(27):8680-9. PMID:15236576

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