1g1m: Difference between revisions

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New page: left|200px<br /><applet load="1g1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1m, resolution 2.25Å" /> '''ALL-FERROUS NITROGEN...
 
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[[Image:1g1m.jpg|left|200px]]<br /><applet load="1g1m" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g1m, resolution 2.25&Aring;" />
'''ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII'''<br />


==Overview==
==ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII==
The structure of the nitrogenase iron protein from Azotobacter vinelandii, in the all-ferrous [4Fe-4S](0) form has been determined to 2.25 A, resolution by using the multiwavelength anomalous diffraction (MAD), phasing technique. The structure demonstrates that major conformational, changes are not necessary either in the iron protein or in the cluster to, accommodate cluster reduction to the [4Fe-4S](0) oxidation state. A survey, of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of, known structure reveals that the [4Fe-4S] cluster of the iron protein has, the largest accessible surface area, suggesting that solvent exposure may, be relevant to the ability of the iron protein to exist in three oxidation, states.
<StructureSection load='1g1m' size='340' side='right'caption='[[1g1m]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1g1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1M 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1g1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1m OCA], [https://pdbe.org/1g1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1m RCSB], [https://www.ebi.ac.uk/pdbsum/1g1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NIFH1_AZOVI NIFH1_AZOVI] The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein.[HAMAP-Rule:MF_00533]
== 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/g1/1g1m_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=1g1m ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1G1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1M OCA].
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii., Strop P, Takahara PM, Chiu H, Angove HC, Burgess BK, Rees DC, Biochemistry. 2001 Jan 23;40(3):651-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11170381 11170381]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Nitrogenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Angove HC]]
[[Category: Angove, H.C.]]
[[Category: Burgess BK]]
[[Category: Burgess, B.K.]]
[[Category: Chiu H-J]]
[[Category: Chiu, H.J.]]
[[Category: Rees DC]]
[[Category: Rees, D.C.]]
[[Category: Strop P]]
[[Category: Strop, P.]]
[[Category: Takahara PM]]
[[Category: Takahara, P.M.]]
[[Category: SF4]]
[[Category: all-ferrous]]
[[Category: iron protein]]
[[Category: nitrogenase]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:37:29 2007''

Latest revision as of 10:21, 7 February 2024

ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDIIALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

Structural highlights

1g1m is a 2 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NIFH1_AZOVI The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein.[HAMAP-Rule:MF_00533]

Evolutionary Conservation

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

See Also

1g1m, resolution 2.25Å

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