1b54

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(New page: 200px<br /><applet load="1b54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b54, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT'''<br />
'''CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT'''<br />
==Overview==
==Overview==
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Yeast hypothetical protein YBL036C (SWISS-PROT P38197), initially thought, to be a member of an 11-protein family, was selected for crystal structure, determination since no structural or functional information was available., The structure has been determined independently by MIR and MAD methods to, 2.0 A resolution. The MAD structure was determined largely through, automated model building. The protein folds as a TIM barrel beginning with, a long N-terminal helix, in contrast to the classic triose phosphate, isomerase (TIM) structure, which begins with a beta-strand. A cofactor, pyridoxal 5'-phosphate, is covalently bound near the C-terminal end of the, barrel, the usual active site in TIM-barrel folds. A single-domain, monomeric molecule, this yeast protein resembles the N-terminal domain of, alanine racemase or ornithine decarboxylase, both of which are two-domain, dimeric proteins. The yeast protein has been shown to have amino-acid, racemase activity. Although selected as a member of a protein family, having no obvious relationship to proteins of known structure, the protein, fold turned out to be a well known and widely distributed fold. This, points to the need for a more comprehensive base of structural information, and better structure-modeling tools before the goal of structure, prediction from amino-acid sequences can be realised. In this case, similarity to a known structure allowed inferences to be made about the, structure and function of a widely distributed protein family.
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Yeast hypothetical protein YBL036C (SWISS-PROT P38197), initially thought to be a member of an 11-protein family, was selected for crystal structure determination since no structural or functional information was available. The structure has been determined independently by MIR and MAD methods to 2.0 A resolution. The MAD structure was determined largely through automated model building. The protein folds as a TIM barrel beginning with a long N-terminal helix, in contrast to the classic triose phosphate isomerase (TIM) structure, which begins with a beta-strand. A cofactor, pyridoxal 5'-phosphate, is covalently bound near the C-terminal end of the barrel, the usual active site in TIM-barrel folds. A single-domain monomeric molecule, this yeast protein resembles the N-terminal domain of alanine racemase or ornithine decarboxylase, both of which are two-domain dimeric proteins. The yeast protein has been shown to have amino-acid racemase activity. Although selected as a member of a protein family having no obvious relationship to proteins of known structure, the protein fold turned out to be a well known and widely distributed fold. This points to the need for a more comprehensive base of structural information and better structure-modeling tools before the goal of structure prediction from amino-acid sequences can be realised. In this case, similarity to a known structure allowed inferences to be made about the structure and function of a widely distributed protein family.
==About this Structure==
==About this Structure==
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1B54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B54 OCA].
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1B54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B54 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
[[Category: Eswaramoorthy, S.]]
[[Category: Eswaramoorthy, S.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
[[Category: PLP]]
[[Category: PLP]]
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[[Category: yeast hypothetical protein]]
[[Category: yeast hypothetical protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:22:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:35 2008''

Revision as of 09:51, 21 February 2008

Image:1b54.gif

1b54, resolution 2.1Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT

Overview

Yeast hypothetical protein YBL036C (SWISS-PROT P38197), initially thought to be a member of an 11-protein family, was selected for crystal structure determination since no structural or functional information was available. The structure has been determined independently by MIR and MAD methods to 2.0 A resolution. The MAD structure was determined largely through automated model building. The protein folds as a TIM barrel beginning with a long N-terminal helix, in contrast to the classic triose phosphate isomerase (TIM) structure, which begins with a beta-strand. A cofactor, pyridoxal 5'-phosphate, is covalently bound near the C-terminal end of the barrel, the usual active site in TIM-barrel folds. A single-domain monomeric molecule, this yeast protein resembles the N-terminal domain of alanine racemase or ornithine decarboxylase, both of which are two-domain dimeric proteins. The yeast protein has been shown to have amino-acid racemase activity. Although selected as a member of a protein family having no obvious relationship to proteins of known structure, the protein fold turned out to be a well known and widely distributed fold. This points to the need for a more comprehensive base of structural information and better structure-modeling tools before the goal of structure prediction from amino-acid sequences can be realised. In this case, similarity to a known structure allowed inferences to be made about the structure and function of a widely distributed protein family.

About this Structure

1B54 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a yeast hypothetical protein selected by a structural genomics approach., Eswaramoorthy S, Gerchman S, Graziano V, Kycia H, Studier FW, Swaminathan S, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):127-35. Epub 2002, Dec 19. PMID:12499548

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