2dfw
From Proteopedia
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|PDB= 2dfw |SIZE=350|CAPTION= <scene name='initialview01'>2dfw</scene>, resolution 2.44Å | |PDB= 2dfw |SIZE=350|CAPTION= <scene name='initialview01'>2dfw</scene>, resolution 2.44Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:34:12 2008'' |
Revision as of 23:34, 30 March 2008
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| , resolution 2.44Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutaminase, with EC number 3.5.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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