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| | {{STRUCTURE_2asf| PDB=2asf | SCENE= }} | | {{STRUCTURE_2asf| PDB=2asf | SCENE= }} |
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| - | '''Crystal structure of the conserved hypothetical protein Rv2074 from Mycobacterium tuberculosis 1.6 A'''
| + | ===Crystal structure of the conserved hypothetical protein Rv2074 from Mycobacterium tuberculosis 1.6 A=== |
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| - | ==Overview==
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| - | The crystal structure of a conserved hypothetical protein corresponding to open reading frame Rv2074 from Mycobacterium tuberculosis (Mtb) has been solved by the two-wavelength anomalous dispersion method. Refinement of the molecular structure at 1.6 angstroms resolution resulted in an R(work) of 0.178 and an R(free) of 0.204. The crystal asymmetric unit contains an Rv2074 monomer; however, the crystallographic twofold symmetry operation of space group P4(3)2(1)2 generates dimeric Rv2074. Each monomer folds into a six-stranded antiparallel beta-barrel flanked by two alpha-helices. The three-dimensional structure of Rv2074 is very similar to that of Mtb Rv1155, a probable pyridoxine 5'-phosphate oxidase (PNPOx), which corroborates well with the relatively high sequence similarity (52%) between the two. A structural comparison between Rv2074 and Rv1155 revealed that the core structure (a six-stranded beta-barrel) is also well conserved; the major differences between the two lie in the N- and C-termini and in the small helical domain. Two citric acid molecules were observed in the active site of Rv2074, the crystals of which were grown in 0.2 M sodium citrate buffer pH 5.0. The citric acid molecules are bound to Rv2074 by hydrogen-bonding interactions with Thr55, Gln60 and Lys61. One of the two citric acid molecules occupies the same spatial position that corresponds to the position of the phosphate and ribose sugar moieties of the flavin mononucleotide (FMN) in the Mtb Rv1155-FMN, Escherichia coli PNPOx-FMN and human PNPOx-FMN complex structures. Owing to its extensive structural similarity with Mtb Rv1155 and to the E. coli and human PNPOx enzymes, Rv2074 may be involved in the final step in the biosynthesis of pyridoxal 5'-phosphate (PLP; a vitamin B6).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16880544}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16880544 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16880544}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tb structural genomics consortium]] | | [[Category: Tb structural genomics consortium]] |
| | [[Category: Tbsgc]] | | [[Category: Tbsgc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:25:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:17:50 2008'' |
Revision as of 11:17, 28 July 2008
Template:STRUCTURE 2asf
Crystal structure of the conserved hypothetical protein Rv2074 from Mycobacterium tuberculosis 1.6 A
Template:ABSTRACT PUBMED 16880544
About this Structure
2ASF is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The molecular structure of Rv2074, a probable pyridoxine 5'-phosphate oxidase from Mycobacterium tuberculosis, at 1.6 angstroms resolution., Biswal BK, Au K, Cherney MM, Garen C, James MN, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):735-42. Epub 2006 Jul 24. PMID:16880544
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