3kbb: Difference between revisions
Jump to navigation
Jump to search
m Protected "3kbb" [edit=sysop:move=sysop] |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Function== | ==Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima== | ||
<StructureSection load='3kbb' size='340' side='right' caption='[[3kbb]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kbb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. 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 THEMA])</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://pdbe.org/3kbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kbb RCSB], [http://www.ebi.ac.uk/pdbsum/3kbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kbb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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. | [[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. | ||
== 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/main_output.php?pdb_ID=3kbb 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[Category: | <div class="pdbe-citations 3kbb" style="background-color:#fffaf0;"></div> | ||
[[Category: Antonyuk, S V | == References == | ||
[[Category: Bessho, Y | <references/> | ||
[[Category: Ellis, M J | __TOC__ | ||
[[Category: Hasnain, S S | </StructureSection> | ||
[[Category: Kuramitsu, S | [[Category: Thema]] | ||
[[Category: | [[Category: Antonyuk, S V]] | ||
[[Category: Strange, R W | [[Category: Bessho, Y]] | ||
[[Category: Yokoyama, S | [[Category: Ellis, M J]] | ||
[[Category: Hasnain, S S]] | |||
[[Category: Kuramitsu, S]] | |||
[[Category: Structural genomic]] | |||
[[Category: Strange, R W]] | |||
[[Category: Yokoyama, S]] | |||
[[Category: Arbohydrate metabolism]] | [[Category: Arbohydrate metabolism]] | ||
[[Category: Cobalt]] | [[Category: Cobalt]] | ||
| Line 29: | Line 52: | ||
[[Category: Nickel]] | [[Category: Nickel]] | ||
[[Category: Nppsfa]] | [[Category: Nppsfa]] | ||
[[Category: Rsgi]] | [[Category: Rsgi]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
Latest revision as of 11:30, 1 November 2017
Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritimaCrystal structure of putative beta-phosphoglucomutase from Thermotoga maritima
Structural highlights
Function[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. 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 PubMedThe 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
|
| ||||||||||||||||||||