1ycf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ycf.gif|left|200px]]<br /><applet load="1ycf" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ycf.gif|left|200px]]
-
caption="1ycf, resolution 3.00&Aring;" />
+
 
-
'''Oxidized (di-ferric) FprA from Moorella thermoacetica'''<br />
+
{{Structure
 +
|PDB= 1ycf |SIZE=350|CAPTION= <scene name='initialview01'>1ycf</scene>, resolution 3.00&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene> and <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Oxidized (di-ferric) FprA from Moorella thermoacetica'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1YCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=FEO:'>FEO</scene>, <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCF OCA].
+
1YCF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCF OCA].
==Reference==
==Reference==
-
X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase., Silaghi-Dumitrescu R, Kurtz DM Jr, Ljungdahl LG, Lanzilotta WN, Biochemistry. 2005 May 3;44(17):6492-501. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15850383 15850383]
+
X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase., Silaghi-Dumitrescu R, Kurtz DM Jr, Ljungdahl LG, Lanzilotta WN, Biochemistry. 2005 May 3;44(17):6492-501. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15850383 15850383]
[[Category: Moorella thermoacetica]]
[[Category: Moorella thermoacetica]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 24: Line 33:
[[Category: scavenging nitric oxide reductase]]
[[Category: scavenging nitric oxide reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:53 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:05 2008''

Revision as of 13:21, 20 March 2008


PDB ID 1ycf

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



Oxidized (di-ferric) FprA from Moorella thermoacetica


Overview

Several members of a widespread class of bacterial and archaeal metalloflavoproteins, called FprA, likely function as scavenging nitric oxide reductases (S-NORs). However, the only published X-ray crystal structure of an FprA is for a protein characterized as a rubredoxin:dioxygen oxidoreductase (ROO) from Desulfovibrio gigas. Therefore, the crystal structure of Moorella thermoacetica FprA, which has been established to function as an S-NOR, was solved in three different states: as isolated, reduced, and reduced, NO-reacted. As is the case for D. gigas ROO, the M. thermoacetica FprA contains a solvent-bridged non-heme, non-sulfur diiron site with five-coordinate iron centers bridged by an aspartate, and terminal glutamate, aspartate, and histidine ligands. However, the M. thermoacetica FprA diiron site showed four His ligands, two to each iron, in all three states, whereas the D. gigas ROO diiron site was reported to contain only three His ligands, even though the fourth His residue is conserved. The Fe1-Fe2 distance within the diiron site of M. thermoacetica FprA remained at 3.2-3.4 A with little or no movement of the protein ligands in the three different states and with conservation of the two proximal open coordination sites. Molecular modeling indicated that each open coordination site can accommodate an end-on NO. This relatively rigid and symmetrical diiron site structure is consistent with formation of a diferrous dinitrosyl as the committed catalytic intermediate leading to formation of N(2)O. These results provide new insight into the structural features that fine-tune biological non-heme diiron sites for dioxygen activation vs nitric oxide reduction.

About this Structure

1YCF is a Single protein structure of sequence from Moorella thermoacetica. Full crystallographic information is available from OCA.

Reference

X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase., Silaghi-Dumitrescu R, Kurtz DM Jr, Ljungdahl LG, Lanzilotta WN, Biochemistry. 2005 May 3;44(17):6492-501. PMID:15850383

Page seeded by OCA on Thu Mar 20 15:21:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools