2x0k

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of modular FAD synthetase from Corynebacterium ammoniagenes

Structural highlights

2x0k is a 2 chain structure with sequence from Corynebacterium ammoniagenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RIBF_CORAM

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 crystal structure of the modular flavin adenine dinucleotide (FAD) synthetase from Corynebacterium ammoniagenes has been solved at 1.95 A resolution. The structure of C. ammoniagenes FAD synthetase presents two catalytic modules-a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide (FMN) adenylyltransferase activity-that are responsible for the synthesis of FAD from riboflavin in two sequential steps. In the monomeric structure, the active sites from both modules are placed 40 A away, preventing the direct transfer of the product from the first reaction (FMN) to the second catalytic site, where it acts as substrate. Crystallographic and biophysical studies revealed a hexameric assembly formed by the interaction of two trimers. Each trimer presents a head-tail configuration, with FMN adenylyltransferase and riboflavin kinase modules from different protomers approaching the active sites and allowing the direct transfer of FMN. Experimental results provide molecular-level evidences of the mechanism of the synthesis of FMN and FAD in prokaryotes in which the oligomeric state could be involved in the regulation of the catalytic efficiency of the modular enzyme.

Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes.,Herguedas B, Martinez-Julvez M, Frago S, Medina M, Hermoso JA J Mol Biol. 2010 Jul 9;400(2):218-30. Epub 2010 May 13. PMID:20471397^[1]

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

References

↑ Herguedas B, Martinez-Julvez M, Frago S, Medina M, Hermoso JA. Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes. J Mol Biol. 2010 Jul 9;400(2):218-30. Epub 2010 May 13. PMID:20471397 doi:10.1016/j.jmb.2010.05.018

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/2x0k"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x0k' size='340' side='right'caption='[[2x0k]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_ammoniagenes"_cooke_and_keith_1927 "bacterium ammoniagenes" cooke and keith 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0K FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0k OCA], [https://pdbe.org/2x0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0k RCSB], [https://www.ebi.ac.uk/pdbsum/2x0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0k ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RIBF_CORAM RIBF_CORAM]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium ammoniagenes cooke and keith 1927]]
+[[Category: Corynebacterium ammoniagenes]]
 [[Category: Large Structures]]
-[[Category: Frago, S]]
+[[Category: Frago S]]
-[[Category: Herguedas, B]]
+[[Category: Herguedas B]]
-[[Category: Hermoso, J A]]
+[[Category: Hermoso JA]]
-[[Category: Martinez-Julvez, M]]
+[[Category: Martinez-Julvez M]]
-[[Category: Medina, M]]
+[[Category: Medina M]]
-[[Category: Atp-binding]]
-[[Category: Multifunctional enzyme]]
-[[Category: Nucleotide-binding]]
-[[Category: Nucleotidyltransferase]]
-[[Category: Riboflavin kinase]]
-[[Category: Transferase]]

2x0k

From Proteopedia

Current revision

Crystal structure of modular FAD synthetase from Corynebacterium ammoniagenes

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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