This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3kbb

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 15:20, 24 December 2014

Crystal 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

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 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

↑ 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

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/3kbb"

@@ Line 8: / Line 8: @@
 <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>
+== 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3kbb

From Proteopedia

Revision as of 15:20, 24 December 2014

Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox