Shwachman-Bodian-Diamond Syndrome Protein
From Proteopedia
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=='''Structure'''== | =='''Structure'''== | ||
{{STRUCTURE_1t95 | PDB=1T95 | SCENE=Sandbox_178/Sbds/4}} | {{STRUCTURE_1t95 | PDB=1T95 | SCENE=Sandbox_178/Sbds/4}} | ||
| - | The structure of the Archaeoglobulus fulgidus SBDS protein orthologue has been determined at the resolution of 1.9 angstroms that showcases a three domain architecture <ref name="one">PMID: 15701631</ref>. The domain that has many disease mutations is the | + | The structure of the Archaeoglobulus fulgidus SBDS protein orthologue has been determined at the resolution of 1.9 angstroms that showcases a three domain architecture <ref name="one">PMID: 15701631</ref>. The domain that has many disease mutations is the N-terminal domain; containing a mixed alpha/beta fold. The central domain has a three-helical bundle, and the C-terminal domain has a ferredoxin-like fold <ref name="one">PMID:15701631</ref>. |
The Archaeoglobus fugidus othrologue of the human SBDS protein (AfSBDS) is a monomer of 240 amino acid residues with water molecules consisting of three domains <ref name="one">PMID:15701631</ref>. Domain I is a N-terminal domain consisting of residues 5-87. Domain II is a central domain consisting of residues 86-161. Domain III is a C-terminal domain consisting of residues 162-234 <ref name="one">PMID:15701631</ref>. This has been described as a V-shaped molecule with an overall dimension of about 54x59x73 Å <ref name="one">PMID:15701631</ref>. A central cavity (about 10 Å deep and 24 Å long) is created at the interface of the three domains <ref name="one">PMID:15701631</ref>. Domain I is a mixed αβ topology consisting of four β strands and four α helices arranged as a 3-stranded anti-parallel β sheets. Helices α1 and α2, along with the intervening loop, line the face of the cleft between Domains I and III <ref name="one">PMID:15701631</ref>. | The Archaeoglobus fugidus othrologue of the human SBDS protein (AfSBDS) is a monomer of 240 amino acid residues with water molecules consisting of three domains <ref name="one">PMID:15701631</ref>. Domain I is a N-terminal domain consisting of residues 5-87. Domain II is a central domain consisting of residues 86-161. Domain III is a C-terminal domain consisting of residues 162-234 <ref name="one">PMID:15701631</ref>. This has been described as a V-shaped molecule with an overall dimension of about 54x59x73 Å <ref name="one">PMID:15701631</ref>. A central cavity (about 10 Å deep and 24 Å long) is created at the interface of the three domains <ref name="one">PMID:15701631</ref>. Domain I is a mixed αβ topology consisting of four β strands and four α helices arranged as a 3-stranded anti-parallel β sheets. Helices α1 and α2, along with the intervening loop, line the face of the cleft between Domains I and III <ref name="one">PMID:15701631</ref>. | ||
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The structure of the orthologue for the human SBDS protein from ''A. fulgidus'' (AfSBDS) has been determined because of the significant amount of amino acid conservation between the two <ref name="one">PMID:15701631</ref>. It had been hypothesized that by doing so, clues could be obtained as to what the function of the protein may be, as well as being able to determine the effects of the mutations found in SDS <ref name="one">PMID:15701631</ref>. | The structure of the orthologue for the human SBDS protein from ''A. fulgidus'' (AfSBDS) has been determined because of the significant amount of amino acid conservation between the two <ref name="one">PMID:15701631</ref>. It had been hypothesized that by doing so, clues could be obtained as to what the function of the protein may be, as well as being able to determine the effects of the mutations found in SDS <ref name="one">PMID:15701631</ref>. | ||
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Revision as of 04:27, 31 March 2010
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
Contents |
Shwachman-Bodian-Diamond Syndrome Protein
Overview
The human Shwachman-Bodian-Diamond syndrome(SBDS) protein belongs to a very conserved family of proteins of unknown function; orthologues found in Archaea, as well as plants and other eukaryotes [1][2]. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism [1]. Two groups of SBDS orthologues have been identified. Archaea, animals, and fungi have SBDS proteins with approximately 250 amino acid residues. However, SBDS protein of plants and protists has the C-terminal extensions around 100 to 250 amino acid residues [3].
Structure
Template:STRUCTURE 1t95 The structure of the Archaeoglobulus fulgidus SBDS protein orthologue has been determined at the resolution of 1.9 angstroms that showcases a three domain architecture [1]. The domain that has many disease mutations is the N-terminal domain; containing a mixed alpha/beta fold. The central domain has a three-helical bundle, and the C-terminal domain has a ferredoxin-like fold [1].
The Archaeoglobus fugidus othrologue of the human SBDS protein (AfSBDS) is a monomer of 240 amino acid residues with water molecules consisting of three domains [1]. Domain I is a N-terminal domain consisting of residues 5-87. Domain II is a central domain consisting of residues 86-161. Domain III is a C-terminal domain consisting of residues 162-234 [1]. This has been described as a V-shaped molecule with an overall dimension of about 54x59x73 Å [1]. A central cavity (about 10 Å deep and 24 Å long) is created at the interface of the three domains [1]. Domain I is a mixed αβ topology consisting of four β strands and four α helices arranged as a 3-stranded anti-parallel β sheets. Helices α1 and α2, along with the intervening loop, line the face of the cleft between Domains I and III [1].
Domain I is also called the FYSH (Fungal, Yhr087wp, Shwachwan) domain because of its distinctive structural homology with a single domain protein Yhr087wp from S. cerevisiae [1]. Yhr087wp is non-essential, localizing to both the nucleus and cytoplasam of yeast cells, and has a role in RNA metabolism [1]. Most mutations of the SBDS protein are found to occur in this domain. Domain II is a compact three-helical bundle structurally similar to the junction recognition site of E. coli [1]. Domain III is made of a four-stranded anti-parallel β-sheet with two α helices packing against the concave surface of the sheet [1]. The βαββαβ folding topology is a ferredoxin-like fold which is usually seen in many RNA binding proteins, including nuclear ribonucleoproteins and small nuclear ribonucleoproteins [1].
The structure of the orthologue for the human SBDS protein from A. fulgidus (AfSBDS) has been determined because of the significant amount of amino acid conservation between the two [1]. It had been hypothesized that by doing so, clues could be obtained as to what the function of the protein may be, as well as being able to determine the effects of the mutations found in SDS [1].
References
- ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 Shammas C, Menne TF, Hilcenko C, Michell SR, Goyenechea B, Boocock GR, Durie PR, Rommens JM, Warren AJ. Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome. J Biol Chem. 2005 May 13;280(19):19221-9. Epub 2005 Feb 8. PMID:15701631 doi:http://dx.doi.org/10.1074/jbc.M414656200
- ↑ Savchenko A, Krogan N, Cort JR, Evdokimova E, Lew JM, Yee AA, Sanchez-Pulido L, Andrade MA, Bochkarev A, Watson JD, Kennedy MA, Greenblatt J, Hughes T, Arrowsmith CH, Rommens JM, Edwards AM. The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism. J Biol Chem. 2005 May 13;280(19):19213-20. Epub 2005 Feb 8. PMID:15701634 doi:10.1074/jbc.M414421200
- ↑ de Oliveira JF, Castilho BA, Sforca ML, Krieger MA, Zeri AC, Guimaraes BG, Zanchin NI. Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. Biochimie. 2009 Apr;91(4):475-83. Epub 2008 Dec 16. PMID:19121363 doi:10.1016/j.biochi.2008.12.001
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