1hmo: Difference between revisions

Latest revision as of 06:06, 13 August 2026

THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION

Structural highlights

1hmo is a 4 chain structure with sequence from Themiste dyscritum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	ACE, FEO, OXY
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HEMT_THEDY Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.

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 PubMed

The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. Restrained least-squares refinement has produced molecular models giving R-values of 16.8% for deoxy (41,064 reflections from 10 A to 2.0 A) and 17.3% for oxy hemerythrin (40,413 reflections from 10.0 A to 2.0 A). The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. The binuclear complex in each derivative retains an oxygen atom bridging the two iron atoms, but the bond lengths found in deoxy hemerythrin support the idea that, in that form, the bridge is protonated, i.e. the bridging group is a hydroxyl. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom.

Structures of deoxy and oxy hemerythrin at 2.0 A resolution.,Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:2016748^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE. Structures of deoxy and oxy hemerythrin at 2.0 A resolution. J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:2016748

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE. Structures of deoxy and oxy hemerythrin at 2.0 A resolution. J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:2016748

[1]

@@ Line 1: / Line 1: @@
 ==THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION==
-<StructureSection load='1hmo' size='340' side='right' caption='[[1hmo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1hmo' size='340' side='right'caption='[[1hmo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hmo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendrostomum_dyscritum Dendrostomum dyscritum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HMO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hmo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmo OCA], [http://pdbe.org/1hmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hmo RCSB], [http://www.ebi.ac.uk/pdbsum/1hmo PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmo OCA], [https://pdbe.org/1hmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmo RCSB], [https://www.ebi.ac.uk/pdbsum/1hmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY]] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
+[https://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
 == 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/hm/1hmo_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hmo_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Dendrostomum dyscritum]]
+[[Category: Large Structures]]
-[[Category: Holmes, M A]]
+[[Category: Themiste dyscritum]]
-[[Category: Letrong, I]]
+[[Category: Holmes MA]]
-[[Category: Sieker, L C]]
+[[Category: Letrong I]]
-[[Category: Stenkamp, R E]]
+[[Category: Sieker LC]]
-[[Category: Turley, S]]
+[[Category: Stenkamp RE]]
-[[Category: Oxygen transport]]
+[[Category: Turley S]]

1hmo: Difference between revisions

Latest revision as of 06:06, 13 August 2026

THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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