4heq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:51, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='4heq' size='340' side='right'caption='[[4heq]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='4heq' size='340' side='right'caption='[[4heq]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4heq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEQ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4heq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megalodesulfovibrio_gigas Megalodesulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEQ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 1.3&#8491;</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=4heq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heq OCA], [http://pdbe.org/4heq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4heq RCSB], [http://www.ebi.ac.uk/pdbsum/4heq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4heq ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=4heq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heq OCA], [https://pdbe.org/4heq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4heq RCSB], [https://www.ebi.ac.uk/pdbsum/4heq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4heq ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/FLAV_MEGG1 FLAV_MEGG1] Electron-transfer proteins that function in various electron transport systems in microorganisms. Functionally interchangeable with ferredoxin.
-
Flavodoxins, which exist widely in microorganisms, have been found in various pathways with multiple physiological functions. The flavodoxin (Fld) containing the cofactor flavin mononucleotide (FMN) from sulfur-reducing bacteria Desulfovibrio gigas (D. gigas) is a short-chain enzyme that comprises 146 residues with a molecular mass of 15 kDa and plays important roles in the electron-transfer chain. To investigate its structure, we purified this Fld directly from anaerobically grown D. gigas cells. The crystal structure of Fld, determined at resolution 1.3 A, is a dimer with two FMN packing in an orientation head to head at a distance of 17 A, which generates a long and connected negatively charged region. Two loops, Thr59-Asp63 and Asp95-Tyr100, are located in the negatively charged region and between two FMN, and are structurally dynamic. An analysis of each monomer shows that the structure of Fld is in a semiquinone state; the positions of FMN and the surrounding residues in the active site deviate. The crystal structure of Fld from D. gigas agrees with a dimeric form in the solution state. The dimerization area, dynamic characteristics and structure variations between monomers enable us to identify a possible binding area for its functional partners.
+
-
 
+
-
Crystal Structure of Dimeric Flavodoxin from Desulfovibrio gigas Suggests a Potential Binding Region for the Electron-Transferring Partner.,Hsieh YC, Chia TS, Fun HK, Chen CJ Int J Mol Sci. 2013 Jan 15;14(1):1667-83. doi: 10.3390/ijms14011667. PMID:23322018<ref>PMID:23322018</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4heq" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Flavodoxin|Flavodoxin]]
+
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Desulfovibrio gigas]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chen, C J]]
+
[[Category: Megalodesulfovibrio gigas]]
-
[[Category: Hsieh, Y C]]
+
[[Category: Chen CJ]]
-
[[Category: Cytoplasma]]
+
[[Category: Hsieh YC]]
-
[[Category: Electron transfer]]
+
-
[[Category: Electron transport]]
+

Current revision

The crystal structure of flavodoxin from Desulfovibrio gigas

PDB ID 4heq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools