2gnw: Difference between revisions
New page: left|200px<br /> <applet load="2gnw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gnw, resolution 2.400Å" /> '''Crystal structure ... |
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[[Image:2gnw.gif|left|200px]]<br /> | [[Image:2gnw.gif|left|200px]]<br /><applet load="2gnw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2gnw, resolution 2.400Å" /> | caption="2gnw, resolution 2.400Å" /> | ||
'''Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40W'''<br /> | '''Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40W'''<br /> | ||
==Overview== | ==Overview== | ||
All plants contain an unusual class of hemoglobins that display | All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet are able to bind exogenous ligands such as oxygen. Structurally homologous hexacoordinate hemoglobins (hxHbs) are also found in animals (neuroglobin and cytoglobin) and some cyanobacteria, where they are thought to play a role in free radical scavenging or ligand sensing. The plant hxHbs can be distinguished from the others because they are only weakly hexcacoordinate in the ferrous state, yet no structural mechanism for regulating hexacoordination has been articulated to account for this behavior. Plant hxHbs contain a conserved Phe at position B10 (Phe(B10)), which is near the reversibly coordinated distal His(E7). We have investigated the effects of Phe(B10) mutation on kinetic and equilibrium constants for hexacoordination and exogenous ligand binding in the ferrous and ferric oxidation states. Kinetic and equilibrium constants for hexacoordination and ligand binding along with CO-FTIR spectroscopy, midpoint reduction potentials, and the crystal structures of two key mutant proteins (F40W and F40L) reveal that Phe(B10) is an important regulatory element in hexacoordination. We show that Phe at this position is the only amino acid that facilitates stable oxygen binding to the ferrous Hb and the only one that promotes ligand binding in the ferric oxidation states. This work presents a structural mechanism for regulating reversible intramolecular coordination in plant hxHbs. | ||
==About this Structure== | ==About this Structure== | ||
2GNW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2GNW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GNW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hoy, J | [[Category: Hoy, J A.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: 2 on 2 helical fold]] | [[Category: 2 on 2 helical fold]] | ||
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[[Category: rice]] | [[Category: rice]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:34 2008'' | ||
Revision as of 18:33, 21 February 2008
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Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40W
OverviewOverview
All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet are able to bind exogenous ligands such as oxygen. Structurally homologous hexacoordinate hemoglobins (hxHbs) are also found in animals (neuroglobin and cytoglobin) and some cyanobacteria, where they are thought to play a role in free radical scavenging or ligand sensing. The plant hxHbs can be distinguished from the others because they are only weakly hexcacoordinate in the ferrous state, yet no structural mechanism for regulating hexacoordination has been articulated to account for this behavior. Plant hxHbs contain a conserved Phe at position B10 (Phe(B10)), which is near the reversibly coordinated distal His(E7). We have investigated the effects of Phe(B10) mutation on kinetic and equilibrium constants for hexacoordination and exogenous ligand binding in the ferrous and ferric oxidation states. Kinetic and equilibrium constants for hexacoordination and ligand binding along with CO-FTIR spectroscopy, midpoint reduction potentials, and the crystal structures of two key mutant proteins (F40W and F40L) reveal that Phe(B10) is an important regulatory element in hexacoordination. We show that Phe at this position is the only amino acid that facilitates stable oxygen binding to the ferrous Hb and the only one that promotes ligand binding in the ferric oxidation states. This work presents a structural mechanism for regulating reversible intramolecular coordination in plant hxHbs.
About this StructureAbout this Structure
2GNW is a Single protein structure of sequence from Oryza sativa with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Role of phenylalanine B10 in plant nonsymbiotic hemoglobins., Smagghe BJ, Kundu S, Hoy JA, Halder P, Weiland TR, Savage A, Venugopal A, Goodman M, Premer S, Hargrove MS, Biochemistry. 2006 Aug 15;45(32):9735-45. PMID:16893175
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