1q89

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(New page: 200px<br /><applet load="1q89" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q89, resolution 2.75&Aring;" /> '''Crystal structure of...)
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[[Image:1q89.gif|left|200px]]<br /><applet load="1q89" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1q89.gif|left|200px]]<br /><applet load="1q89" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q89, resolution 2.75&Aring;" />
caption="1q89, resolution 2.75&Aring;" />
'''Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (cubic crystal form)'''<br />
'''Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (cubic crystal form)'''<br />
==Overview==
==Overview==
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Transcription start site selection in eukaryotes is mediated through, combinations of the TATA, initiator (Inr), and downstream promoter, elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate, thought to represent an ancient eukaryote lineage, the Inr appears to be, solely responsible for start site selection and is recognized by the, initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr, binding domain (IBD) connected via a flexible linker to a C-terminal, domain (C domain). Here we present crystal structures of the apoIBD and, IBD-Inr complexes and the C domain. The IBD structures reveal a, winged-helix motif with prokaryotic and eukaryotic features and a scaffold, similar to that of ETS-family proteins. The C domain structure and, biochemical studies indicate that it interacts with the T. vaginalis RNAP, II large subunit C-terminal domain. These data suggest that binding of, IBP39 to the Inr directly recruits RNAP II and in this way initiates, transcription.
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Transcription start site selection in eukaryotes is mediated through combinations of the TATA, initiator (Inr), and downstream promoter elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate thought to represent an ancient eukaryote lineage, the Inr appears to be solely responsible for start site selection and is recognized by the initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr binding domain (IBD) connected via a flexible linker to a C-terminal domain (C domain). Here we present crystal structures of the apoIBD and IBD-Inr complexes and the C domain. The IBD structures reveal a winged-helix motif with prokaryotic and eukaryotic features and a scaffold similar to that of ETS-family proteins. The C domain structure and biochemical studies indicate that it interacts with the T. vaginalis RNAP II large subunit C-terminal domain. These data suggest that binding of IBP39 to the Inr directly recruits RNAP II and in this way initiates transcription.
==About this Structure==
==About this Structure==
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1Q89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q89 OCA].
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1Q89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q89 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trichomonas vaginalis]]
[[Category: Trichomonas vaginalis]]
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[[Category: Johnson, P.J.]]
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[[Category: Johnson, P J.]]
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[[Category: Schumacher, M.A.]]
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[[Category: Schumacher, M A.]]
[[Category: core promoter]]
[[Category: core promoter]]
[[Category: initator binding protein]]
[[Category: initator binding protein]]
[[Category: inr]]
[[Category: inr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:45:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:51 2008''

Revision as of 12:36, 21 February 2008


1q89, resolution 2.75Å

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Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (cubic crystal form)

Overview

Transcription start site selection in eukaryotes is mediated through combinations of the TATA, initiator (Inr), and downstream promoter elements (DPE). In Trichomonas vaginalis, a parabasalian flagellate thought to represent an ancient eukaryote lineage, the Inr appears to be solely responsible for start site selection and is recognized by the initiator binding protein 39 kDa (IBP39). IBP39 contains an N-terminal Inr binding domain (IBD) connected via a flexible linker to a C-terminal domain (C domain). Here we present crystal structures of the apoIBD and IBD-Inr complexes and the C domain. The IBD structures reveal a winged-helix motif with prokaryotic and eukaryotic features and a scaffold similar to that of ETS-family proteins. The C domain structure and biochemical studies indicate that it interacts with the T. vaginalis RNAP II large subunit C-terminal domain. These data suggest that binding of IBP39 to the Inr directly recruits RNAP II and in this way initiates transcription.

About this Structure

1Q89 is a Single protein structure of sequence from Trichomonas vaginalis. Full crystallographic information is available from OCA.

Reference

Structural basis of core promoter recognition in a primitive eukaryote., Schumacher MA, Lau AO, Johnson PJ, Cell. 2003 Nov 14;115(4):413-24. PMID:14622596

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