3kbb: Difference between revisions

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{{STRUCTURE_3kbb| PDB=3kbb | SCENE= }}
==Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima==
===Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima===
<StructureSection load='3kbb' size='340' side='right' caption='[[3kbb]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
{{ABSTRACT_PUBMED_20054115}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3kbb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pib 2pib]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KBB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bpgm, tm_1254 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8])</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=3kbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kbb RCSB], [http://www.ebi.ac.uk/pdbsum/3kbb PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/3kbb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of TM1254, a putative beta-phosphoglucomutase from T. maritima, was determined to 1.74 A resolution in a high-throughput structural genomics programme. Diffraction data were obtained from crystals belonging to space group P22(1)2(1), with unit-cell parameters a = 48.16, b = 66.70, c = 83.80 A, and were refined to an R factor of 19.2%. The asymmetric unit contained one protein molecule which is comprised of two domains. Structural homologues were found from protein databases that confirmed a strong resemblance between TM1254 and members of the haloacid dehalogenase (HAD) hydrolase family.


==Function==
Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.,Strange RW, Antonyuk SV, Ellis MJ, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1218-21. Epub 2009 Nov 27. PMID:20054115<ref>PMID:20054115</ref>
[[http://www.uniprot.org/uniprot/P1254_THEMA P1254_THEMA]] Displays high phosphatase activity toward erythrose 4-phosphate, fructose 6-phosphate, 2-deoxyglucose 6-phosphate, and mannose 6-phosphate. May have a role in the intracellular metabolism of many phosphorylated carbohydrates.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3kbb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pib 2pib]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KBB OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020054115</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Thermotoga maritima msb8]]
[[Category: Thermotoga maritima msb8]]
[[Category: Antonyuk, S V.]]
[[Category: Antonyuk, S V]]
[[Category: Bessho, Y.]]
[[Category: Bessho, Y]]
[[Category: Ellis, M J.]]
[[Category: Ellis, M J]]
[[Category: Hasnain, S S.]]
[[Category: Hasnain, S S]]
[[Category: Kuramitsu, S.]]
[[Category: Kuramitsu, S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Structural genomic]]
[[Category: Strange, R W.]]
[[Category: Strange, R W]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S]]
[[Category: Arbohydrate metabolism]]
[[Category: Arbohydrate metabolism]]
[[Category: Cobalt]]
[[Category: Cobalt]]
Line 29: Line 48:
[[Category: Nickel]]
[[Category: Nickel]]
[[Category: Nppsfa]]
[[Category: Nppsfa]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]

Revision as of 19:11, 18 December 2014

Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritimaCrystal structure of putative beta-phosphoglucomutase from Thermotoga maritima

Structural highlights

3kbb is a 1 chain structure with sequence from Thermotoga maritima msb8. This structure supersedes the now removed PDB entry 2pib. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Gene:bpgm, tm_1254 (Thermotoga maritima MSB8)
Resources:FirstGlance, OCA, RCSB, PDBsum

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 structure of TM1254, a putative beta-phosphoglucomutase from T. maritima, was determined to 1.74 A resolution in a high-throughput structural genomics programme. Diffraction data were obtained from crystals belonging to space group P22(1)2(1), with unit-cell parameters a = 48.16, b = 66.70, c = 83.80 A, and were refined to an R factor of 19.2%. The asymmetric unit contained one protein molecule which is comprised of two domains. Structural homologues were found from protein databases that confirmed a strong resemblance between TM1254 and members of the haloacid dehalogenase (HAD) hydrolase family.

Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.,Strange RW, Antonyuk SV, Ellis MJ, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1218-21. Epub 2009 Nov 27. PMID:20054115[1]

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

References

  1. ↑ Strange RW, Antonyuk SV, Ellis MJ, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS. Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1218-21. Epub 2009 Nov 27. PMID:20054115 doi:10.1107/S1744309109046302

3kbb, resolution 1.74Å

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