1y30

From Proteopedia

(Difference between revisions)

Revision as of 14:43, 24 December 2014

X-ray crystal structure of mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase complexed with flavin mononucleotide at 2.2 a resolution

Structural highlights

1y30 is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1xxo, 2aq6
Gene:	Rv1155 (Mycobacterium tuberculosis)
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Function

[O06553_MYCTU] Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (Potential).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The X-ray crystal structure of a conserved hypothetical protein of molecular weight 16.3 kDa from Mycobacterium tuberculosis corresponding to open reading frame (ORF) Rv1155 has been solved by the multiwavelength anomalous dispersion method and refined at 1.8 A resolution. The crystal structure revealed that Rv1155 is a dimer in the crystal and that each monomer folds into a large and a small domain; the large domain is a six-stranded antiparallel beta-barrel flanked by two small alpha-helices and the small domain is a helix-loop-helix motif. The dimer interface is formed by residues protruding primarily from five of the six beta-strands in each subunit. Based on structural similarity and on ligand binding, it has been established that Rv1155 is a pyridoxine 5'-phosphate oxidase, the Escherichia coli and human counterparts of which catalyse the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino-acid metabolism. The structures of flavin mononucleotide (FMN) and pyridoxal 5'-phosphate (PLP) bound separately to Rv1155 have been determined at 2.2 and 1.7 A resolution, respectively. Only one monomer binds non-covalently to one FMN molecule or to one PLP molecule. Arg55 and Lys57 are the key residues making hydrogen bonds and ionic interactions with the phosphate and ribose groups of the FMN molecule, whereas Arg55 and Arg129 provide hydrogen bonds and ionic interactions with the phosphate group of the PLP. Structural comparisons of Rv1155 from M. tuberculosis with its E. coli and human counterparts demonstrate that the core structure is highly conserved and the FMN-binding site is similarly disposed in each of the structures.

Structures of Mycobacterium tuberculosispyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate.,Biswal BK, Cherney MM, Wang M, Garen C, James MN Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1492-9. Epub 2005, Oct 19. PMID:16239726^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Biswal BK, Cherney MM, Wang M, Garen C, James MN. Structures of Mycobacterium tuberculosispyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1492-9. Epub 2005, Oct 19. PMID:16239726 doi:10.1107/S0907444905026673

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y30"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1y30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y30 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xxo|1xxo]], [[2aq6|2aq6]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xxo|1xxo]], [[2aq6|2aq6]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y30 RCSB], [http://www.ebi.ac.uk/pdbsum/1y30 PDBsum], [http://www.topsan.org/Proteins/TBSGC/1y30 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y30 RCSB], [http://www.ebi.ac.uk/pdbsum/1y30 PDBsum], [http://www.topsan.org/Proteins/TBSGC/1y30 TOPSAN]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/O06553_MYCTU O06553_MYCTU]] Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (Potential).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Biswal, B K.]]
+[[Category: Biswal, B K]]
-[[Category: Cherney, M M.]]
+[[Category: Cherney, M M]]
-[[Category: Garen, C.]]
+[[Category: Garen, C]]
-[[Category: James, M N.]]
+[[Category: James, M N]]
-[[Category: TBSGC, TB Structural Genomics Consortium.]]
+[[Category: Structural genomic]]
-[[Category: Wang, M.]]
+[[Category: Wang, M]]
 [[Category: Flavin mononucleotide]]
 [[Category: Oxidoreductase]]
-[[Category: Protein structure initiative]]
+[[Category: PSI, Protein structure initiative]]
-[[Category: Psi]]
-[[Category: Structural genomic]]
-[[Category: Tb structural genomics consortium]]
 [[Category: Tbsgc]]

1y30

From Proteopedia

Revision as of 14:43, 24 December 2014

X-ray crystal structure of mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase complexed with flavin mononucleotide at 2.2 a resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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