2dfw
From Proteopedia
(New page: 200px<br /><applet load="2dfw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dfw, resolution 2.44Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Glutaminase of Micrococcus luteus K-3 (intact glutaminase; 48kDa) is | + | 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== | ==About this Structure== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:21 2008'' |
Revision as of 14:58, 21 February 2008
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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. Active as Glutaminase, with EC number 3.5.1.2 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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