1g1m: Difference between revisions
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==ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII== | ==ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII== | ||
<StructureSection load='1g1m' size='340' side='right' caption='[[1g1m]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='1g1m' size='340' side='right'caption='[[1g1m]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g1m]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1M FirstGlance]. <br> | <table><tr><td colspan='2'>[[1g1m]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1M FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1g1m" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1g1m" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Nitrogenase|Nitrogenase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Large Structures]] | |||
[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
[[Category: Angove, H C]] | [[Category: Angove, H C]] | ||
Revision as of 12:15, 23 October 2019
ALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDIIALL-FERROUS NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII
Structural highlights
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. Publication Abstract from PubMedThe 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. 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:11170381[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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