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1kr7

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Revision as of 06:34, 18 August 2021

Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus

Structural highlights

1kr7 is a 1 chain structure with sequence from Cerla. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLBN_CERLA] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min.

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

A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.

The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold.,Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M Structure. 2002 May;10(5):725-35. PMID:12015154^[1]

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

References

↑ Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M. The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold. Structure. 2002 May;10(5):725-35. PMID:12015154

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kr7"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kr7' size='340' side='right'caption='[[1kr7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kr7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cerla Cerla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KR7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cerla Cerla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KR7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kr7 OCA], [http://pdbe.org/1kr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kr7 RCSB], [http://www.ebi.ac.uk/pdbsum/1kr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kr7 ProSAT]</span></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=1kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kr7 OCA], [https://pdbe.org/1kr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kr7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLBN_CERLA GLBN_CERLA]] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min.
+[[https://www.uniprot.org/uniprot/GLBN_CERLA GLBN_CERLA]] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kr7

From Proteopedia

Revision as of 06:34, 18 August 2021

Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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