1nog
From Proteopedia
(New page: 200px<br /><applet load="1nog" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nog, resolution 1.55Å" /> '''Crystal Structure of...) |
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| - | [[Image:1nog.gif|left|200px]]<br /><applet load="1nog" size=" | + | [[Image:1nog.gif|left|200px]]<br /><applet load="1nog" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nog, resolution 1.55Å" /> | caption="1nog, resolution 1.55Å" /> | ||
'''Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum'''<br /> | '''Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ATP:cobalamin adenosyltransferase MMAB was recently identified as the gene | + | ATP:cobalamin adenosyltransferase MMAB was recently identified as the gene responsible for a disorder of cobalamin metabolism in humans (cblB complementation group). The crystal structure of the MMAB sequence homologue from Thermoplasma acidophilum (TA1434; GenBank identification number gi|16082403) was determined to a resolution of 1.5 A. TA1434 was confirmed to be an ATP:cobalamin adenosyltransferase, which depended absolutely on divalent metal ions (Mg2+ > Mn2+ > Co2+) and only used ATP or dATP as adenosyl donors. The apparent Km of TA1434 was 110 microM (kcat = 0.23 s(-1)) for ATP, 140 microM (kcat = 0.11 s(-1)) for dATP, and 3 microM (kcat = 0.18 s(-1)) for cobalamin. TA1434 is a trimer in solution and in the crystal structure, with each subunit composed of a five-helix bundle. The location of disease-related point mutations and other residues conserved among the homologues of TA1434 suggest that the active site lies at the junctions between the subunits. Mutations in TA1434 that correspond to the disease-related mutations resulted in proteins that were inactive for ATP:cobalamin adenosyltransferase activity in vitro, confirming that these mutations define the molecular basis of the human disease. |
==About this Structure== | ==About this Structure== | ||
| - | 1NOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http:// | + | 1NOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
[[Category: Christendat, D.]] | [[Category: Christendat, D.]] | ||
| - | [[Category: Edwards, A | + | [[Category: Edwards, A M.]] |
[[Category: Gu, J.]] | [[Category: Gu, J.]] | ||
[[Category: Iakounine, A.]] | [[Category: Iakounine, A.]] | ||
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Pennycooke, M.]] | [[Category: Pennycooke, M.]] | ||
[[Category: Sanishvili, R.]] | [[Category: Sanishvili, R.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:14 2008'' |
Revision as of 12:08, 21 February 2008
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Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum
Overview
ATP:cobalamin adenosyltransferase MMAB was recently identified as the gene responsible for a disorder of cobalamin metabolism in humans (cblB complementation group). The crystal structure of the MMAB sequence homologue from Thermoplasma acidophilum (TA1434; GenBank identification number gi|16082403) was determined to a resolution of 1.5 A. TA1434 was confirmed to be an ATP:cobalamin adenosyltransferase, which depended absolutely on divalent metal ions (Mg2+ > Mn2+ > Co2+) and only used ATP or dATP as adenosyl donors. The apparent Km of TA1434 was 110 microM (kcat = 0.23 s(-1)) for ATP, 140 microM (kcat = 0.11 s(-1)) for dATP, and 3 microM (kcat = 0.18 s(-1)) for cobalamin. TA1434 is a trimer in solution and in the crystal structure, with each subunit composed of a five-helix bundle. The location of disease-related point mutations and other residues conserved among the homologues of TA1434 suggest that the active site lies at the junctions between the subunits. Mutations in TA1434 that correspond to the disease-related mutations resulted in proteins that were inactive for ATP:cobalamin adenosyltransferase activity in vitro, confirming that these mutations define the molecular basis of the human disease.
About this Structure
1NOG is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
The structural basis for methylmalonic aciduria. The crystal structure of archaeal ATP:cobalamin adenosyltransferase., Saridakis V, Yakunin A, Xu X, Anandakumar P, Pennycooke M, Gu J, Cheung F, Lew JM, Sanishvili R, Joachimiak A, Arrowsmith CH, Christendat D, Edwards AM, J Biol Chem. 2004 May 28;279(22):23646-53. Epub 2004 Mar 25. PMID:15044458
Page seeded by OCA on Thu Feb 21 14:08:14 2008
Categories: Single protein | Thermoplasma acidophilum | Arrowsmith, C H. | Christendat, D. | Edwards, A M. | Gu, J. | Iakounine, A. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Pennycooke, M. | Sanishvili, R. | Saridakis, V. | Xu, X. | Mcsg | Midwest center for structural genomics | Protein structure initiative | Psi | Structural genomics
