1hr3: Difference between revisions

Revision as of 14:04, 21 February 2008

STRUCTURE OF TRIMERIC HAEMERYTHRIN

OverviewOverview

Several simplifying structural principles have been developed from the considerable data contained in the three-dimensional structures of proteins determined in the past two decades. One of these is based on the observation that particular folding motifs often occur in a variety of structural and functional settings. The compact bundle of four antiparallel alpha-helices, first seen in the structure of myohaemerythrin, is an example. Several non-haemerythrin proteins have since been found to have the same folding pattern, and haemerythrins themselves exist in a wide variety of quaternary arrangements. The unusual ability of the haemerythrin fold to associate as dimers, trimers, tetramers, octamers or higher aggregates provides an opportunity for examining structural diversity in subunit association. We have used X-ray crystallography to study the subunit structure of trimeric haemerythrin from a Siphonosoma species. We report here that the pattern of intersubunit helix-helix interactions differs from the most common mode of association of other helix-bundle proteins. In a novel approach to structure analysis at low resolution, experimental phases for the structure determination were based on anomalous scattering from the iron atoms native to haemerythrin, using the new resolved-anomalous phasing procedure.

About this StructureAbout this Structure

1HR3 is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of trimeric haemerythrin., Smith JL, Hendrickson WA, Addison AW, Nature. 1983 May 5-11;303(5912):86-8. PMID:6843663

Page seeded by OCA on Thu Feb 21 13:04:02 2008

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OCA

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-[[Image:1hr3.jpg|left|200px]]<br /><applet load="1hr3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hr3.jpg|left|200px]]<br /><applet load="1hr3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hr3, resolution 5.5&Aring;" />
 '''STRUCTURE OF TRIMERIC HAEMERYTHRIN'''<br />
 ==Overview==
-Several simplifying structural principles have been developed from the, considerable data contained in the three-dimensional structures of, proteins determined in the past two decades. One of these is based on the, observation that particular folding motifs often occur in a variety of, structural and functional settings. The compact bundle of four, antiparallel alpha-helices, first seen in the structure of, myohaemerythrin, is an example. Several non-haemerythrin proteins have, since been found to have the same folding pattern, and haemerythrins, themselves exist in a wide variety of quaternary arrangements. The unusual, ability of the haemerythrin fold to associate as dimers, trimers, tetramers, octamers or higher aggregates provides an opportunity for, examining structural diversity in subunit association. We have used X-ray, crystallography to study the subunit structure of trimeric haemerythrin, from a Siphonosoma species. We report here that the pattern of, intersubunit helix-helix interactions differs from the most common mode of, association of other helix-bundle proteins. In a novel approach to, structure analysis at low resolution, experimental phases for the, structure determination were based on anomalous scattering from the iron, atoms native to haemerythrin, using the new resolved-anomalous phasing, procedure.
+Several simplifying structural principles have been developed from the considerable data contained in the three-dimensional structures of proteins determined in the past two decades. One of these is based on the observation that particular folding motifs often occur in a variety of structural and functional settings. The compact bundle of four antiparallel alpha-helices, first seen in the structure of myohaemerythrin, is an example. Several non-haemerythrin proteins have since been found to have the same folding pattern, and haemerythrins themselves exist in a wide variety of quaternary arrangements. The unusual ability of the haemerythrin fold to associate as dimers, trimers, tetramers, octamers or higher aggregates provides an opportunity for examining structural diversity in subunit association. We have used X-ray crystallography to study the subunit structure of trimeric haemerythrin from a Siphonosoma species. We report here that the pattern of intersubunit helix-helix interactions differs from the most common mode of association of other helix-bundle proteins. In a novel approach to structure analysis at low resolution, experimental phases for the structure determination were based on anomalous scattering from the iron atoms native to haemerythrin, using the new resolved-anomalous phasing procedure.
 ==About this Structure==
-HR3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with FEA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HR3 OCA].
+HR3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=FEA:'>FEA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR3 OCA].
 ==Reference==
 Structure of trimeric haemerythrin., Smith JL, Hendrickson WA, Addison AW, Nature. 1983 May 5-11;303(5912):86-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6843663 6843663]
 [[Category: Protein complex]]
-[[Category: Addison, A.W.]]
+[[Category: Addison, A W.]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson, W A.]]
-[[Category: Smith, J.L.]]
+[[Category: Smith, J L.]]
 [[Category: FEA]]
 [[Category: oxygen transport protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:57:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:02 2008''