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[[Image:1ahn.gif|left|200px]]<br />
<applet load="1ahn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ahn, resolution 2.6&Aring;" />
'''E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION'''<br />


==Overview==
==E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION==
In Escherichia coli, flavodoxin is the physiological electron donor for, the reductive activation of the enzymes pyruvate formate-lyase, anaerobic, ribonucleotide reductase, and B12-dependent methionine synthase. As a, basis for studies of the interactions of flavodoxin with methionine, synthase, crystal structures of orthorhombic and trigonal forms of, oxidized recombinant flavodoxin from E. coli have been determined. The, orthorhombic form (space group P2(1)2(1)2(1), a = 126.4, b = 41.10, c =, 69.15 A, with two molecules per asymmetric unit) was solved initially by, molecular replacement at a resolution of 3.0 A, using coordinates from the, structure of the flavodoxin from Synechococcus PCC 7942 (Anacystis, nidulans). Data extending to 1.8-A resolution were collected at 140 K and, the structure was refined to an Rwork of 0.196 and an Rfree of 0.250 for, reflections with I &gt; 0. The final model contains 3,224 non-hydrogen atoms, per asymmetric unit, including 62 flavin mononucleotide (FMN) atoms, 354, water molecules, four calcium ions, four sodium ions, two chloride ions, and two Bis-Tris buffer molecules. The structure of the protein in the, trigonal form (space group P312, a = 78.83, c = 52.07 A) was solved by, molecular replacement using the coordinates from the orthorhombic, structure, and was refined with all data from 10.0 to 2.6 A (R = 0.191;, Rfree = 0.249). The sequence Tyr 58-Tyr 59, in a bend near the FMN, has so, far been found only in the flavodoxins from E. coli and Haemophilus, influenzae, and may be important in interactions of flavodoxin with its, partners in activation reactions. The tyrosine residues in this bend are, influenced by intermolecular contacts and adopt different orientations in, the two crystal forms. Structural comparisons with flavodoxins from, Synechococcus PCC 7942 and Anaebaena PCC 7120 suggest other residues that, may also be critical for recognition by methionine synthase.
<StructureSection load='1ahn' size='340' side='right'caption='[[1ahn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ahn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=1ahn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahn OCA], [https://pdbe.org/1ahn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahn RCSB], [https://www.ebi.ac.uk/pdbsum/1ahn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLAV_ECOLI FLAV_ECOLI] Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase.<ref>PMID:9730838</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/1ahn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ahn ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: FMN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHN OCA].
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
 
== References ==
==Reference==
<references/>
A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution., Hoover DM, Ludwig ML, Protein Sci. 1997 Dec;6(12):2525-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9416602 9416602]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hoover, D.M.]]
[[Category: Hoover DM]]
[[Category: Ludwig, M.L.]]
[[Category: Ludwig ML]]
[[Category: CA]]
[[Category: FMN]]
[[Category: electron transport]]
[[Category: flavodoxin]]
[[Category: flavoprotein]]
[[Category: reductive activation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 14:04:32 2007''

Latest revision as of 09:30, 7 February 2024

E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTIONE. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION

Structural highlights

1ahn is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLAV_ECOLI Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Jarrett JT, Hoover DM, Ludwig ML, Matthews RG. The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme. Biochemistry. 1998 Sep 8;37(36):12649-58. PMID:9730838 doi:http://dx.doi.org/10.1021/bi9808565

1ahn, resolution 2.60Å

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