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2ig3

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Crystal structure of group III truncated hemoglobin from Campylobacter jejuni

Structural highlights

2ig3 is a 2 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.15Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRHBP_CAMJE Has been suggested to be involved in cytochrome c peroxidase or P450-like oxygen chemistry or cyanide detoxification. The high oxygen affinity of this protein suggests that it probably does not function as an oxygen transporter.

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

Truncated hemoglobins (trHbs) constitute a distinct lineage in the globin superfamily, distantly related in size and fold to myoglobin and monomeric hemoglobins. Their phylogenetic analyses revealed that three groups (I, II, and III) compose the trHb family. Group I and II trHbs adopt a simplified globin fold, essentially composed of a 2-on-2 alpha-helical sandwich, wrapped around the heme group. So far no structural data have been reported for group III trHbs. Here we report the three-dimensional structure of the group III trHbP from the eubacterium Campylobacter jejuni. The 2.15-A resolution crystal structure of C. jejuni trHbP (cyano-met form) shows that the 2-on-2 trHb fold is substantially conserved in the trHb group III, despite the absence of the Gly-based sequence motifs that were considered necessary for the attainment of the trHb specific fold. The heme crevice presents important structural modifications in the C-E region and in the FG helical hinge, with novel surface clefts at the proximal heme site. Contrary to what has been observed for group I and II trHbs, no protein matrix tunnel/cavity system is evident in C. jejuni trHbP. A gating movement of His(E7) side chain (found in two alternate conformations in the crystal structure) may be instrumental for ligand entry to the heme distal site. Sequence conservation allows extrapolating part of the structural results here reported to the whole trHb group III.

Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni.,Nardini M, Pesce A, Labarre M, Richard C, Bolli A, Ascenzi P, Guertin M, Bolognesi M J Biol Chem. 2006 Dec 8;281(49):37803-12. Epub 2006 Oct 5. PMID:17023416^[1]

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

References

↑ Nardini M, Pesce A, Labarre M, Richard C, Bolli A, Ascenzi P, Guertin M, Bolognesi M. Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni. J Biol Chem. 2006 Dec 8;281(49):37803-12. Epub 2006 Oct 5. PMID:17023416 doi:10.1074/jbc.M607254200

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/2ig3"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ig3' size='340' side='right'caption='[[2ig3]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ig3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IG3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ig3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IG3 FirstGlance]. <br>
-</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=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ux8|1ux8]], [[1dly|1dly]], [[1dlw|1dlw]], [[1idr|1idr]], [[1s69|1s69]], [[1ngk|1ngk]]</div></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=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctb ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</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=2ig3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ig3 OCA], [https://pdbe.org/2ig3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ig3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ig3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ig3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TRHBP_CAMJE TRHBP_CAMJE]] Has been suggested to be involved in cytochrome c peroxidase or P450-like oxygen chemistry or cyanide detoxification. The high oxygen affinity of this protein suggests that it probably does not function as an oxygen transporter.
+[https://www.uniprot.org/uniprot/TRHBP_CAMJE TRHBP_CAMJE] Has been suggested to be involved in cytochrome c peroxidase or P450-like oxygen chemistry or cyanide detoxification. The high oxygen affinity of this protein suggests that it probably does not function as an oxygen transporter.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Campylobacter fetus subsp. jejuni smibert 1974]]
+[[Category: Campylobacter jejuni]]
 [[Category: Large Structures]]
-[[Category: Ascenzi, P]]
+[[Category: Ascenzi P]]
-[[Category: Bolognesi, M]]
+[[Category: Bolognesi M]]
-[[Category: Guertin, M]]
+[[Category: Guertin M]]
-[[Category: Labarre, M]]
+[[Category: Labarre M]]
-[[Category: Nardini, M]]
+[[Category: Nardini M]]
-[[Category: Pesce, A]]
+[[Category: Pesce A]]
-[[Category: 2-on-2 globin]]
-[[Category: Oxygen storage-transport complex]]
-[[Category: Truncated hemoglobin]]

2ig3

From Proteopedia

Current revision

Crystal structure of group III truncated hemoglobin from Campylobacter jejuni

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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