1t6n

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(New page: 200px<br /> <applet load="1t6n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6n, resolution 1.94&Aring;" /> '''Crystal structure o...)
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caption="1t6n, resolution 1.94&Aring;" />
'''Crystal structure of the N-terminal domain of human UAP56'''<br />
'''Crystal structure of the N-terminal domain of human UAP56'''<br />
==Overview==
==Overview==
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UAP56 is an essential eukaryotic pre-mRNA splicing factor and mRNA export, factor. The mechanisms of its functions are not well understood. We, determined the crystal structures of the N- and C-terminal domains of, human UAP56 (comprising 90% of the full-length UAP56) at 1.9 A resolution., The two domains each have a RecA-like fold and are connected by a flexible, linker. The overall fold of each domain is highly similar to the, corresponding domains of eIF4A (a prototypic DExD/H-box protein), with, differences at the loops and termini. This structural similarity suggests, that UAP56 is likely to possess ATPase and helicase activity similar to, eIF4A. The NTP binding pocket of UAP56 is occupied by a citrate ion, mimicking the phosphates of NTP and retaining the P loop in an open, conformation. The crystal structure of the N-terminal domain of UAP56 also, reveals a dimer interface that is potentially important for UAP56's, function.
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UAP56 is an essential eukaryotic pre-mRNA splicing factor and mRNA export factor. The mechanisms of its functions are not well understood. We determined the crystal structures of the N- and C-terminal domains of human UAP56 (comprising 90% of the full-length UAP56) at 1.9 A resolution. The two domains each have a RecA-like fold and are connected by a flexible linker. The overall fold of each domain is highly similar to the corresponding domains of eIF4A (a prototypic DExD/H-box protein), with differences at the loops and termini. This structural similarity suggests that UAP56 is likely to possess ATPase and helicase activity similar to eIF4A. The NTP binding pocket of UAP56 is occupied by a citrate ion, mimicking the phosphates of NTP and retaining the P loop in an open conformation. The crystal structure of the N-terminal domain of UAP56 also reveals a dimer interface that is potentially important for UAP56's function.
==About this Structure==
==About this Structure==
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1T6N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FLC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6N OCA].
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1T6N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FLC:'>FLC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6N OCA].
==Reference==
==Reference==
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[[Category: reca-like fold]]
[[Category: reca-like fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:21:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:24 2008''

Revision as of 13:10, 21 February 2008


1t6n, resolution 1.94Å

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Crystal structure of the N-terminal domain of human UAP56

Overview

UAP56 is an essential eukaryotic pre-mRNA splicing factor and mRNA export factor. The mechanisms of its functions are not well understood. We determined the crystal structures of the N- and C-terminal domains of human UAP56 (comprising 90% of the full-length UAP56) at 1.9 A resolution. The two domains each have a RecA-like fold and are connected by a flexible linker. The overall fold of each domain is highly similar to the corresponding domains of eIF4A (a prototypic DExD/H-box protein), with differences at the loops and termini. This structural similarity suggests that UAP56 is likely to possess ATPase and helicase activity similar to eIF4A. The NTP binding pocket of UAP56 is occupied by a citrate ion, mimicking the phosphates of NTP and retaining the P loop in an open conformation. The crystal structure of the N-terminal domain of UAP56 also reveals a dimer interface that is potentially important for UAP56's function.

About this Structure

1T6N is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export., Zhao R, Shen J, Green MR, MacMorris M, Blumenthal T, Structure. 2004 Aug;12(8):1373-81. PMID:15296731

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