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2dfw

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[[Image:2dfw.gif|left|200px]]
[[Image:2dfw.gif|left|200px]]
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{{Structure
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|PDB= 2dfw |SIZE=350|CAPTION= <scene name='initialview01'>2dfw</scene>, resolution 2.44&Aring;
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The line below this paragraph, containing "STRUCTURE_2dfw", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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/Glutaminase Glutaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.2 3.5.1.2] </span>
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{{STRUCTURE_2dfw| PDB=2dfw | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfw OCA], [http://www.ebi.ac.uk/pdbsum/2dfw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dfw RCSB]</span>
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'''Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3'''
'''Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3'''
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[[Category: Wakayama, M.]]
[[Category: Wakayama, M.]]
[[Category: Yoshimune, K.]]
[[Category: Yoshimune, K.]]
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[[Category: alpha/beta structure]]
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[[Category: Alpha/beta structure]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:20:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:34:12 2008''
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Revision as of 21:20, 3 May 2008

Template:STRUCTURE 2dfw

Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3


Overview

Glutaminase of Micrococcus luteus K-3 (intact glutaminase; 48kDa) is digested to a C-terminally truncated fragment (glutaminase fragment; 42kDa) that shows higher salt tolerance than that of the intact glutaminase. The crystal structure of the glutaminase fragment was determined at 2.4A resolution using multiple-wavelength anomalous dispersion (MAD). The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic serine-lysine dyad (S64 and K67) is located in a cleft of the N-terminal domain. Mutations of the S64 or K67 residues abolished the enzyme activity. The N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism. A diffraction analysis of the intact glutaminase crystals (a twinning fraction of 0.43) located the glutaminase fragment in the unit cell but failed to turn up clear densities for the missing C-terminal portion of the molecule.

About this Structure

2DFW is a Single protein structure of sequence from Micrococcus luteus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3., Yoshimune K, Shirakihara Y, Shiratori A, Wakayama M, Chantawannakul P, Moriguchi M, Biochem Biophys Res Commun. 2006 Aug 11;346(4):1118-24. Epub 2006 Jun 6. PMID:16793004 Page seeded by OCA on Sun May 4 00:20:34 2008

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