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3ct6

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Revision as of 21:46, 15 November 2017

Crystal structure of DhaM of L. lactis

Structural highlights

3ct6 is a 2 chain structure with sequence from "bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	dhaM ("Bacterium lactis" Lister 1873)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHAM_LACLA] Phosphotransferase subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaM serves as the phosphoryl donor (By similarity).

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

Bacterial dihydroxyacetone (Dha) kinases do not exchange the ADP for ATP but utilize a subunit of the phosphoenolpyruvate carbohydrate phosphotransferase system for in situ rephosphorylation of a permanently bound ADP-cofactor. Here we report the 2.1-angstroms crystal structure of the transient complex between the phosphotransferase subunit DhaM of the phosphotransferase system and the nucleotide binding subunit DhaL of the Dha kinase of Lactococcus lactis, the 1.1-angstroms structure of the free DhaM dimer, and the 2.5-angstroms structure of the Dha-binding DhaK subunit. Conserved salt bridges and an edge-to-plane stacking contact between two tyrosines serve to orient DhaL relative to the DhaM dimer. The distance between the imidazole Nepsilon2 of the DhaM His-10 and the beta-phosphate oxygen of ADP, between which the gamma-phosphate is transferred, is 4.9 angstroms. An invariant arginine, which is essential for activity, is appropriately positioned to stabilize the gamma-phosphate in the transition state. The (betaalpha)4alpha fold of DhaM occurs a second time as a subfold in the DhaK subunit. By docking DhaL-ADP to this subfold, the nucleotide bound to DhaL and the C1-hydroxyl of Dha bound to DhaK are positioned for in-line transfer of phosphate.

X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex.,Zurbriggen A, Jeckelmann JM, Christen S, Bieniossek C, Baumann U, Erni B J Biol Chem. 2008 Dec 19;283(51):35789-96. Epub 2008 Oct 28. PMID:18957416^[1]

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

References

↑ Zurbriggen A, Jeckelmann JM, Christen S, Bieniossek C, Baumann U, Erni B. X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex. J Biol Chem. 2008 Dec 19;283(51):35789-96. Epub 2008 Oct 28. PMID:18957416 doi:10.1074/jbc.M804893200

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/3ct6"

@@ Line 3: / Line 3: @@
 <StructureSection load='3ct6' size='340' side='right' caption='[[3ct6]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ct6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CT6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ct6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CT6 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</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=3ct6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ct6 OCA], [http://pdbe.org/3ct6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ct6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ct6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ct6 ProSAT]</span></td></tr>
 </table>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Lactococcus lactis]]
+[[Category: Bacterium lactis lister 1873]]
 [[Category: Zurbriggen, A]]
 [[Category: Glycerol metabolism]]

3ct6

From Proteopedia

Revision as of 21:46, 15 November 2017

Crystal structure of DhaM of L. lactis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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