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.

4qih

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 14:50, 5 August 2016

The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase Rv2419c complexes with VO3

Structural highlights

4qih is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4pz9, 4pza
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GPGP_MYCTO] Involved in the biosynthesis of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to glucosylglycerate (GG) (By similarity).

Publication Abstract from PubMed

Mycobacterium tuberculosis (Mtb) synthesizes polymethylated polysaccharides that form complexes with long chain fatty acids. These complexes, referred to as methylglucose lipopolysaccharides (MGLPs), regulate fatty acid biosynthesis in vivo, including biosynthesis of mycolic acids that are essential for building the cell wall. Glucosyl-3-phosphoglycerate phosphatase (GpgP, EC 5.4.2.1), encoded by Rv2419c gene, catalyzes the second step of the pathway for the biosynthesis of MGLPs. The molecular basis for this dephosphorylation is currently not understood. Here, we describe the crystal structures of apo-, vanadate-bound, and phosphate-bound MtbGpgP, depicting unliganded, reaction intermediate mimic, and product-bound views of MtbGpgP, respectively. The enzyme consists of a single domain made up of a central beta-sheet flanked by alpha-helices on either side. The active site is located in a positively charged cleft situated above the central beta-sheet. Unambiguous electron density for vanadate covalently bound to His(11), mimicking the phosphohistidine intermediate, was observed. The role of residues interacting with the ligands in catalysis was probed by site-directed mutagenesis. Arg(10), His(11), Asn(17), Gln(23), Arg(60), Glu(84), His(159), and Leu(209) are important for enzymatic activity. Comparison of the structures of MtbGpgP revealed conformational changes in a key loop region connecting beta1 with alpha1. This loop regulates access to the active site. MtbGpgP functions as dimer. L209E mutation resulted in monomeric GpgP, rendering the enzyme incapable of dephosphorylation. The structures of GpgP reported here are the first crystal structures for histidine-phosphatase-type GpgPs. These structures shed light on a key step in biosynthesis of MGLPs that could be targeted for development of anti-tuberculosis therapeutics.

Mechanism of dephosphorylation of glucosyl-3-phosphoglycerate by a histidine phosphatase.,Zheng Q, Jiang D, Zhang W, Zhang Q, Zhao Q, Jin J, Li X, Yang H, Bartlam M, Shaw N, Zhou W, Rao Z J Biol Chem. 2014 Aug 1;289(31):21242-51. doi: 10.1074/jbc.M114.569913. Epub 2014, Jun 9. PMID:24914210^[1]

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

References

↑ Zheng Q, Jiang D, Zhang W, Zhang Q, Zhao Q, Jin J, Li X, Yang H, Bartlam M, Shaw N, Zhou W, Rao Z. Mechanism of dephosphorylation of glucosyl-3-phosphoglycerate by a histidine phosphatase. J Biol Chem. 2014 Aug 1;289(31):21242-51. doi: 10.1074/jbc.M114.569913. Epub 2014, Jun 9. PMID:24914210 doi:http://dx.doi.org/10.1074/jbc.M114.569913

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qih"

@@ Line 1: / Line 1: @@
 ==The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase Rv2419c complexes with VO3==
 <StructureSection load='4qih' size='340' side='right' caption='[[4qih]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN3:VANADATE+ION'>VN3</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pz9|4pz9]], [[4pza|4pza]]</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=4qih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qih RCSB], [http://www.ebi.ac.uk/pdbsum/4qih PDBsum]</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=4qih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qih OCA], [http://pdbe.org/4qih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qih RCSB], [http://www.ebi.ac.uk/pdbsum/4qih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qih ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qih" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4qih

From Proteopedia

Revision as of 14:50, 5 August 2016

The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase Rv2419c complexes with VO3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox