3msv: Difference between revisions

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<StructureSection load='3msv' size='340' side='right'caption='[[3msv]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
<StructureSection load='3msv' size='340' side='right'caption='[[3msv]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3msv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MSV FirstGlance]. <br>
<table><tr><td colspan='2'>[[3msv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MSV FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPCC4B3.07 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msv OCA], [https://pdbe.org/3msv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3msv RCSB], [https://www.ebi.ac.uk/pdbsum/3msv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3msv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msv OCA], [https://pdbe.org/3msv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3msv RCSB], [https://www.ebi.ac.uk/pdbsum/3msv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3msv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ETT1_SCHPO ETT1_SCHPO]] Required for correct translation termination (By similarity). Positive regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression. Acts also as a direct inhibitor of ofd1. Functions probably by inhibiting the ability of the ofd1 to accelerate Sre1N degradation in absence of oxygen.<ref>PMID:15116432</ref> <ref>PMID:19158663</ref> 
[https://www.uniprot.org/uniprot/ETT1_SCHPO ETT1_SCHPO] Required for correct translation termination (By similarity). Positive regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression. Acts also as a direct inhibitor of ofd1. Functions probably by inhibiting the ability of the ofd1 to accelerate Sre1N degradation in absence of oxygen.<ref>PMID:15116432</ref> <ref>PMID:19158663</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fission yeast protein Sre1, the homolog of the mammalian sterol regulatory element-binding protein (SREBP), is a hypoxic transcription factor required for sterol homeostasis and low-oxygen growth. Nro1 regulates the stability of the N-terminal transcription factor domain of Sre1 (Sre1N) by inhibiting the action of the prolyl 4-hydroxylase-like Ofd1 in an oxygen-dependent manner. The crystal structure of Nro1 determined at 2.2 A resolution shows an all-alpha-helical fold that can be divided into two domains: a small N-terminal domain, and a larger C-terminal HEAT-repeat domain. Follow-up studies showed that Nro1 defines a new class of nuclear import adaptor that functions both in Ofd1 nuclear localization and in the oxygen-dependent inhibition of Ofd1 to control the hypoxic response.
 
The hypoxic regulator of sterol synthesis nro1 is a nuclear import adaptor.,Yeh TL, Lee CY, Amzel LM, Espenshade PJ, Bianchet MA Structure. 2011 Apr 13;19(4):503-14. PMID:21481773<ref>PMID:21481773</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3msv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cbs 356]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Amzel, L M]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Bianchet, M A]]
[[Category: Amzel LM]]
[[Category: Yeh, T L]]
[[Category: Bianchet MA]]
[[Category: Heat repeat]]
[[Category: Yeh TL]]
[[Category: Helix repeat]]
[[Category: Protein binding]]

Latest revision as of 12:58, 14 February 2024

The hypoxic regulator of sterol synthesis Nro1 is a nuclear import adaptorThe hypoxic regulator of sterol synthesis Nro1 is a nuclear import adaptor

Structural highlights

3msv is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.18Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ETT1_SCHPO Required for correct translation termination (By similarity). Positive regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression. Acts also as a direct inhibitor of ofd1. Functions probably by inhibiting the ability of the ofd1 to accelerate Sre1N degradation in absence of oxygen.[1] [2]

References

  1. ↑ Chen XQ, Du X, Liu J, Balasubramanian MK, Balasundaram D. Identification of genes encoding putative nucleoporins and transport factors in the fission yeast Schizosaccharomyces pombe: a deletion analysis. Yeast. 2004 Apr 30;21(6):495-509. PMID:15116432 doi:http://dx.doi.org/10.1002/yea.1115
  2. ↑ Lee CY, Stewart EV, Hughes BT, Espenshade PJ. Oxygen-dependent binding of Nro1 to the prolyl hydroxylase Ofd1 regulates SREBP degradation in yeast. EMBO J. 2009 Jan 21;28(2):135-43. doi: 10.1038/emboj.2008.271. PMID:19158663 doi:http://dx.doi.org/10.1038/emboj.2008.271

3msv, resolution 2.18Å

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