1hqx
From Proteopedia
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|PDB= 1hqx |SIZE=350|CAPTION= <scene name='initialview01'>1hqx</scene>, resolution 3.Å | |PDB= 1hqx |SIZE=350|CAPTION= <scene name='initialview01'>1hqx</scene>, resolution 3.Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1rla|1RLA]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqx OCA], [http://www.ebi.ac.uk/pdbsum/1hqx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hqx RCSB]</span> | ||
}} | }} | ||
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[[Category: Jr., T M.Sossong.]] | [[Category: Jr., T M.Sossong.]] | ||
[[Category: Lavulo, L T.]] | [[Category: Lavulo, L T.]] | ||
| - | [[Category: MN]] | ||
[[Category: arginase]] | [[Category: arginase]] | ||
[[Category: binuclear manganese cluster]] | [[Category: binuclear manganese cluster]] | ||
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[[Category: subunit-subunit interaction]] | [[Category: subunit-subunit interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:17 2008'' |
Revision as of 18:09, 30 March 2008
| |||||||
| , resolution 3.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Arginase, with EC number 3.5.3.1 | ||||||
| Related: | 1RLA
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
R308K ARGINASE VARIANT
Overview
The structure of the trimeric, manganese metalloenzyme, rat liver arginase, has been previously determined at 2.1-A resolution (Kanyo, Z. F., Scolnick, L. R., Ash, D. E., and Christianson, D. W., (1996) Nature 383, 554-557). A key feature of this structure is a novel S-shaped oligomerization motif at the carboxyl terminus of the protein that mediates approximately 54% of the intermonomer contacts. Arg-308, located within this oligomerization motif, nucleates a series of intramonomer and intermonomer salt links. In contrast to the trimeric wild-type enzyme, the R308A, R308E, and R308K variants of arginase exist as monomeric species, as determined by gel filtration and analytical ultracentrifugation, indicating that mutation of Arg-308 shifts the equilibrium for trimer dissociation by at least a factor of 10(5). These monomeric arginase variants are catalytically active, with k(cat)/K(m) values that are 13-17% of the value for wild-type enzyme. The arginase variants are characterized by decreased temperature stability relative to the wild-type enzyme. Differential scanning calorimetry shows that the midpoint temperature for unfolding of the Arg-308 variants is in the range of 63.6-65.5 degrees C, while the corresponding value for the wild-type enzyme is 70 degrees C. The three-dimensional structure of the R308K variant has been determined at 3-A resolution. At the high protein concentrations utilized in the crystallizations, this variant exists as a trimer, but weakened salt link interactions are observed for Lys-308.
About this Structure
1HQX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid., Lavulo LT, Sossong TM Jr, Brigham-Burke MR, Doyle ML, Cox JD, Christianson DW, Ash DE, J Biol Chem. 2001 Apr 27;276(17):14242-8. Epub 2001 Jan 24. PMID:11278703
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