1cqx: Difference between revisions

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New page: left|200px<br /><applet load="1cqx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqx, resolution 1.75Å" /> '''Crystal structure of...
 
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[[Image:1cqx.jpg|left|200px]]<br /><applet load="1cqx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cqx, resolution 1.75&Aring;" />
'''Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution'''<br />


==Overview==
==Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution==
The molecular structure of the flavohemoglobin from Alcaligenes eutrophus, has been determined to a resolution of 1.75 A and refined to an R-factor, of 19.6%. The protein comprises two fused modules: a heme binding module, which belongs to the globin family, and an FAD binding oxidoreductase, module, which adopts a fold like ferredoxin reductase. The most striking, deviation of the bacterial globin structure from those of other species is, the movement of helix E in a way to provide more space in the vicinity of, the distal heme binding site. A comparison with other members of the, ferredoxin reductase family shows similar tertiary structures for the, individual FAD and NAD binding domains but largely different interdomain, orientations. The heme and FAD molecules approach each other to a minimal, distance of 6.3 A and adopt an interplanar angle of 80 degrees. The, electron transfer from FAD to heme occurs in a predominantly polar, environment and may occur directly or be mediated by a water molecule.
<StructureSection load='1cqx' size='340' side='right'caption='[[1cqx]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cqx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQX 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGG:1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL'>DGG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1cqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqx OCA], [https://pdbe.org/1cqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cqx RCSB], [https://www.ebi.ac.uk/pdbsum/1cqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cqx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HMP_CUPNH HMP_CUPNH] Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.  In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.
== 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/cq/1cqx_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=1cqx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CQX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator] with NA, HEM, FAD and DGG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CQX OCA].
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution., Ermler U, Siddiqui RA, Cramm R, Friedrich B, EMBO J. 1995 Dec 15;14(24):6067-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8557026 8557026]
[[Category: Cupriavidus necator]]
[[Category: Cupriavidus necator]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cramm, R.]]
[[Category: Cramm R]]
[[Category: Ermler, U.]]
[[Category: Ermler U]]
[[Category: Friedrich, B.]]
[[Category: Friedrich B]]
[[Category: Siddiqui, R.A.]]
[[Category: Siddiqui RA]]
[[Category: DGG]]
[[Category: FAD]]
[[Category: HEM]]
[[Category: NA]]
[[Category: globin fold]]
[[Category: helix-flanked five-stranded parallel beta sheet]]
[[Category: lipid binding protein]]
[[Category: six-stranded antiparallel beta sheet]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:41:17 2007''

Latest revision as of 09:44, 7 February 2024

Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolutionCrystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution

Structural highlights

1cqx is a 2 chain structure with sequence from Cupriavidus necator. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HMP_CUPNH Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.

Evolutionary Conservation

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

See Also

1cqx, resolution 1.75Å

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