1w0d: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
==The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)==
==The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)==
<StructureSection load='1w0d' size='340' side='right' caption='[[1w0d]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='1w0d' size='340' side='right'caption='[[1w0d]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1w0d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1w0d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1w0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0d OCA], [http://pdbe.org/1w0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0d RCSB], [http://www.ebi.ac.uk/pdbsum/1w0d PDBsum], [http://www.topsan.org/Proteins/XMTB/1w0d TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0d OCA], [https://pdbe.org/1w0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0d RCSB], [https://www.ebi.ac.uk/pdbsum/1w0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0d ProSAT], [https://www.topsan.org/Proteins/XMTB/1w0d TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LEU3_MYCTU LEU3_MYCTU] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0d_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0d_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 33: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 3-isopropylmalate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Janowski, R]]
[[Category: Janowski R]]
[[Category: Kefala, G]]
[[Category: Kefala G]]
[[Category: Mueller-Dieckmann, C]]
[[Category: Mueller-Dieckmann C]]
[[Category: Singh, R K]]
[[Category: Singh RK]]
[[Category: Structural genomic]]
[[Category: Weiss MS]]
[[Category: Weiss, M S]]
[[Category: Dehydrogenase]]
[[Category: Leucine biosynthesis]]
[[Category: Nad]]
[[Category: Oxidoreductase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tb]]
[[Category: Tbsgc]]

Latest revision as of 12:08, 9 May 2024

The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)

Structural highlights

1w0d is a 4 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

LEU3_MYCTU Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035]

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 crystal structure of the enzyme 3-isopropylmalate dehydrogenase (IPMDH) from Mycobacterium tuberculosis (LeuB, Mtb-IPMDH, Rv2995c) without substrate or co-factor was determined at 1.65 A resolution, which is the highest resolution reported for an IPMDH to date. The crystals contain two functional dimers in the asymmetric unit in an arrangement close to a tetramer of D2 symmetry. Despite the absence of a substrate or inhibitor bound to the protein, the structure of the monomer resembles the previously observed closed form of the enzyme more closely than the open form. A comparison with the substrate complex of IPMDH from Thiobacillus ferrooxidans and the co-factor complex of the Thermus thermophilus enzyme revealed a close relationship of the active-site architecture between the various bacterial enzymes. The inhibitor O-isobutenyl oxalylhydroxamate was found to bind to the active site of IPMDH in a mode similar to the substrate isopropylmalate.

The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis.,Singh RK, Kefala G, Janowski R, Mueller-Dieckmann C, von Kries JP, Weiss MS J Mol Biol. 2005 Feb 11;346(1):1-11. Epub 2004 Dec 23. PMID:15663922[1]

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

See Also

References

  1. Singh RK, Kefala G, Janowski R, Mueller-Dieckmann C, von Kries JP, Weiss MS. The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis. J Mol Biol. 2005 Feb 11;346(1):1-11. Epub 2004 Dec 23. PMID:15663922 doi:10.1016/j.jmb.2004.11.059

1w0d, resolution 1.65Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA