1g0b: Difference between revisions
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'''CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5''' | {{Structure | ||
|PDB= 1g0b |SIZE=350|CAPTION= <scene name='initialview01'>1g0b</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1G0B is a [ | 1G0B is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0B OCA]. | ||
==Reference== | ==Reference== | ||
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin., Mueser TC, Rogers PH, Arnone A, Biochemistry. 2000 Dec 19;39(50):15353-64. PMID:[http:// | Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin., Mueser TC, Rogers PH, Arnone A, Biochemistry. 2000 Dec 19;39(50):15353-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11112521 11112521] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protoporphyrin ix]] | [[Category: protoporphyrin ix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:21 2008'' | ||
Revision as of 12:16, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5
OverviewOverview
Initial crystallographic studies suggested that fully liganded mammalian hemoglobin can adopt only a single quaternary structure, the quaternary R structure. However, more recent crystallographic studies revealed the existence of a second quaternary structure for liganded hemoglobin, the quaternary R2 structure. Since these quaternary structures can be crystallized, both must be energetically accessible structures that coexist in solution. Unanswered questions include (i) the relative abundance of the R and R2 structures under various solution conditions and (ii) whether other quaternary structures are energetically accessible for the liganded alpha(2)beta(2) hemoglobin tetramer. Although crystallographic methods cannot directly answer the first question, they represent the most direct and most accurate approach to answering the second question. We now have determined and refined three different crystal structures of bovine carbonmonoxyhemoglobin. These structures provide clear evidence that the dimer-dimer interface of liganded hemoglobin has a wide range of energetically accessible structures that are related to each other by a simple sliding motion. The dimer-dimer interface acts as a "molecular slide bearing" that allows the two alpha beta dimers to slide back and forth without greatly altering the number or the nature of the intersubunit contacts. Since the general stereochemical features of this interface are not unusual, it is likely that interface sliding of the kind displayed by fully liganded hemoglobin plays important structural and functional roles in many other protein assemblies.
About this StructureAbout this Structure
1G0B is a Protein complex structure of sequences from Equus caballus. Full crystallographic information is available from OCA.
ReferenceReference
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin., Mueser TC, Rogers PH, Arnone A, Biochemistry. 2000 Dec 19;39(50):15353-64. PMID:11112521
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