3zhw
From Proteopedia
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| - | + | ==X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their Functional Implications== | |
| - | + | <StructureSection load='3zhw' size='340' side='right' caption='[[3zhw]], [[Resolution|resolution]] 2.22Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3zhw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZHW FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=3zhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zhw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zhw RCSB], [http://www.ebi.ac.uk/pdbsum/3zhw PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/HBL1_ARATH HBL1_ARATH]] May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has an unusually high affinity for O(2) because of a very low dissociation constant. | [[http://www.uniprot.org/uniprot/HBL1_ARATH HBL1_ARATH]] May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has an unusually high affinity for O(2) because of a very low dissociation constant. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Genome of the model dicot flowering plant, Arabidopsis thaliana, a popular tool for understanding molecular biology of plant physiology, encodes all three classes of plant hemoglobins that differ in their sequence, ligand binding and spectral properties. As such these globins are of considerable attention. Crystal structures of few members of plant class I nonsymbiotic hemoglobin have been described earlier. Here we report the crystal structure of Arabidopsis class I hemoglobin (AHb1) to 2.2A and compare its key features with the structures of similar nonsymbiotic hemoglobin from other species. Crystal structure of AHb1 is homologous to the related members with similar globin fold and heme pocket architecture. The structure is homodimeric in the asymmetric unit with both distal and proximal histidines coordinating to the heme iron atom. Residues lining the dimeric interface are also conserved in AHb1 with the exception of additional electrostatic interaction between H112 and E113 of each subunit and that involving Y119 through two water molecules. In addition, differences in heme pocket non-covalent interactions, a novel Ser residue at F7 position, Xe binding site variability, internal cavity topology differences, CD loop conformation and stability and other such properties might explain kinetic variability in AHb1. Detailed cavity analysis of AHb1 showed the presence of a novel long tunnel connecting the distal pockets of both the monomers. Presence of such tunnel, along with conformational heterogeneity observed in the two chains, might suggest cooperative ligand binding and support its role in NO scavenging. This article is part of a Special Issue entitled: Oxygen Binding and Sensing Proteins. | ||
| - | + | X-Ray crystallographic structural characteristics of Arabidopsis hemoglobin I and their functional implications.,Mukhi N, Dhindwal S, Uppal S, Kumar P, Kaur J, Kundu S Biochim Biophys Acta. 2013 Feb 26. pii: S1570-9639(13)00087-3. doi:, 10.1016/j.bbapap.2013.02.024. PMID:23485912<ref>PMID:23485912</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
| - | [[Category: Dhindwal, S | + | [[Category: Dhindwal, S]] |
| - | [[Category: Kaur, J | + | [[Category: Kaur, J]] |
| - | [[Category: Kumar, P | + | [[Category: Kumar, P]] |
| - | [[Category: Kundu, S | + | [[Category: Kundu, S]] |
| - | [[Category: Mukhi, N | + | [[Category: Mukhi, N]] |
| - | [[Category: Uppal, S | + | [[Category: Uppal, S]] |
[[Category: Oxygen binding]] | [[Category: Oxygen binding]] | ||
Revision as of 05:01, 25 December 2014
X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their Functional Implications
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