1r4v: Difference between revisions

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[[Image:1r4v.jpg|left|200px]]<br /><applet load="1r4v" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1r4v.jpg|left|200px]]<br /><applet load="1r4v" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1r4v, resolution 1.90Å" />

'''1.9A crystal structure of protein AQ328 from Aquifex aeolicus'''<br />

==Overview==

The structure of Aq_328, an uncharacterized protein from hyperthermophilic, bacteria Aquifex aeolicus, has been determined to 1.9 A by using, multi-wavelength anomalous diffraction (MAD) phasing. Although the amino, acid sequence analysis shows that Aq_328 has no significant similarity to, proteins with a known structure and function, the structure comparison by, using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E), with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation, equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular, weight of about 20 kDa. The overall architecture of Aq_328 consists of two, noncanonical histone domains in tandem repeat within a single chain, and, is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal, histone heterodimer (HMfA/HMfB). The sequence comparisons between the two, histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate, that most of the conserved residues that underlie the Aq_328 architecture, are used to build and stabilize the two cross-shaped antiparallel histone, domains. The high percentage of salt bridges in the structure could be a, factor in the protein's thermostability. The structural similarities to, other histone-like proteins, molecular properties, and potential function, of Aq_328 are discussed in this paper.

The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that Aq_328 has no significant similarity to proteins with a known structure and function, the structure comparison by using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E) with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular weight of about 20 kDa. The overall architecture of Aq_328 consists of two noncanonical histone domains in tandem repeat within a single chain, and is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal histone heterodimer (HMfA/HMfB). The sequence comparisons between the two histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate that most of the conserved residues that underlie the Aq_328 architecture are used to build and stabilize the two cross-shaped antiparallel histone domains. The high percentage of salt bridges in the structure could be a factor in the protein's thermostability. The structural similarities to other histone-like proteins, molecular properties, and potential function of Aq_328 are discussed in this paper.

==About this Structure==

1R4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with ZN and CAC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1R4V OCA].

1R4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CAC:'>CAC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4V OCA].

==Reference==

Line 17:

[[Category: Kim, Y.]]

[[Category: Kossiakoff, A.]]

[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]

[[Category: MCSG, Midwest Center for Structural Genomics.]]

[[Category: Qiu, Y.]]

[[Category: Tereshko, V.]]

Line 31:

[[Category: structural genomics]]

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@@ Line 1: / Line 1: @@
-[[Image:1r4v.jpg|left|200px]]<br /><applet load="1r4v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1r4v.jpg|left|200px]]<br /><applet load="1r4v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1r4v, resolution 1.90&Aring;" />
 '''1.9A crystal structure of protein AQ328 from Aquifex aeolicus'''<br />
 ==Overview==
-The structure of Aq_328, an uncharacterized protein from hyperthermophilic, bacteria Aquifex aeolicus, has been determined to 1.9 A by using, multi-wavelength anomalous diffraction (MAD) phasing. Although the amino, acid sequence analysis shows that Aq_328 has no significant similarity to, proteins with a known structure and function, the structure comparison by, using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E), with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation, equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular, weight of about 20 kDa. The overall architecture of Aq_328 consists of two, noncanonical histone domains in tandem repeat within a single chain, and, is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal, histone heterodimer (HMfA/HMfB). The sequence comparisons between the two, histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate, that most of the conserved residues that underlie the Aq_328 architecture, are used to build and stabilize the two cross-shaped antiparallel histone, domains. The high percentage of salt bridges in the structure could be a, factor in the protein's thermostability. The structural similarities to, other histone-like proteins, molecular properties, and potential function, of Aq_328 are discussed in this paper.
+The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that Aq_328 has no significant similarity to proteins with a known structure and function, the structure comparison by using the Dali server reveals that it: (1) assumes a histone-like fold, and (2) is similar to an ancestral nuclear histone protein (PDB code 1F1E) with z-score 8.1 and RMSD 3.6 A over 124 residues. A sedimentation equilibrium experiment indicates that Aq_328 is a monomer in solution, with an average sedimentation coefficient of 2.4 and an apparent molecular weight of about 20 kDa. The overall architecture of Aq_328 consists of two noncanonical histone domains in tandem repeat within a single chain, and is similar to eukaryotic heterodimer (H2A/H2B and H3/H4) and an archaeal histone heterodimer (HMfA/HMfB). The sequence comparisons between the two histone domains of Aq_328 and six eukaryotic/archaeal histones demonstrate that most of the conserved residues that underlie the Aq_328 architecture are used to build and stabilize the two cross-shaped antiparallel histone domains. The high percentage of salt bridges in the structure could be a factor in the protein's thermostability. The structural similarities to other histone-like proteins, molecular properties, and potential function of Aq_328 are discussed in this paper.
 ==About this Structure==
-R4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with ZN and CAC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R4V OCA].
+R4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CAC:'>CAC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4V OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Kim, Y.]]
 [[Category: Kossiakoff, A.]]
-[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
+[[Category: MCSG, Midwest Center for Structural Genomics.]]
 [[Category: Qiu, Y.]]
 [[Category: Tereshko, V.]]
@@ Line 31: / Line 31: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:15:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:03 2008''