2pyo: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2pyo.gif|left|200px]]<br /><applet load="2pyo" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2pyo.gif|left|200px]]
caption="2pyo, resolution 2.430&Aring;" />
 
'''Drosophila nucleosome core'''<br />
{{Structure
|PDB= 2pyo |SIZE=350|CAPTION= <scene name='initialview01'>2pyo</scene>, resolution 2.430&Aring;
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+E+1002'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+J+1003'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+J+1009'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+I+1011'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+I+1012'>AC5</scene>, <scene name='pdbsite=AC6:Mn+Binding+Site+For+Residue+I+1013'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+J+1014'>AC7</scene>, <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+H+1015'>AC8</scene>, <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+D+1016'>AC9</scene>, <scene name='pdbsite=BC1:Cl+Binding+Site+For+Residue+A+1017'>BC1</scene> and <scene name='pdbsite=BC2:Cl+Binding+Site+For+Residue+E+1018'>BC2</scene>
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
|ACTIVITY=
|GENE= His3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]), His4, H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]), His2A, H2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]), His2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
}}
 
'''Drosophila nucleosome core'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
2PYO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+E+1002'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+J+1003'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+J+1009'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+I+1011'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+I+1012'>AC5</scene>, <scene name='pdbsite=AC6:Mn+Binding+Site+For+Residue+I+1013'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+J+1014'>AC7</scene>, <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+H+1015'>AC8</scene>, <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+D+1016'>AC9</scene>, <scene name='pdbsite=BC1:Cl+Binding+Site+For+Residue+A+1017'>BC1</scene> and <scene name='pdbsite=BC2:Cl+Binding+Site+For+Residue+E+1018'>BC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYO OCA].  
2PYO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYO OCA].  


==Reference==
==Reference==
Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer., Clapier CR, Chakravarthy S, Petosa C, Fernandez-Tornero C, Luger K, Muller CW, Proteins. 2007 Oct 23;71(1):1-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17957772 17957772]
Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer., Clapier CR, Chakravarthy S, Petosa C, Fernandez-Tornero C, Luger K, Muller CW, Proteins. 2007 Oct 23;71(1):1-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17957772 17957772]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 23: Line 32:
[[Category: structural protein/dna complex]]
[[Category: structural protein/dna complex]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 5 13:25:38 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:19:36 2008''

Revision as of 19:19, 20 March 2008

File:2pyo.gif


PDB ID 2pyo

Drag the structure with the mouse to rotate
, resolution 2.430Å
Sites: , , , , , , , , , and
Ligands: and
Gene: His3 (Drosophila melanogaster), His4, H4 (Drosophila melanogaster), His2A, H2a (Drosophila melanogaster), His2B (Drosophila melanogaster)
Coordinates: save as pdb, mmCIF, xml



Drosophila nucleosome core


OverviewOverview

We determined the 2.45 A crystal structure of the nucleosome core particle from Drosophila melanogaster and compared it to that of Xenopus laevis bound to the identical 147 base-pair DNA fragment derived from human alpha-satellite DNA. Differences between the two structures primarily reflect 16 amino acid substitutions between species, 15 of which are in histones H2A and H2B. Four of these involve histone tail residues, resulting in subtly altered protein-DNA interactions that exemplify the structural plasticity of these tails. Of the 12 substitutions occurring within the histone core regions, five involve small, solvent-exposed residues not involved in intraparticle interactions. The remaining seven involve buried hydrophobic residues, and appear to have coevolved so as to preserve the volume of side chains within the H2A hydrophobic core and H2A-H2B dimer interface. Thus, apart from variations in the histone tails, amino acid substitutions that differentiate Drosophila from Xenopus histones occur in mutually compensatory combinations. This highlights the tight evolutionary constraints exerted on histones since the vertebrate and invertebrate lineages diverged. Proteins 2008. (c) 2007 Wiley-Liss, Inc.

About this StructureAbout this Structure

2PYO is a Protein complex structure of sequences from Drosophila melanogaster and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer., Clapier CR, Chakravarthy S, Petosa C, Fernandez-Tornero C, Luger K, Muller CW, Proteins. 2007 Oct 23;71(1):1-7. PMID:17957772

Page seeded by OCA on Thu Mar 20 18:19:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA