3bg1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==Architecture of a Coat for the Nuclear Pore Membrane==
==Architecture of a Coat for the Nuclear Pore Membrane==
<StructureSection load='3bg1' size='340' side='right' caption='[[3bg1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3bg1' size='340' side='right' caption='[[3bg1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
Line 5: Line 6:
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bg0|3bg0]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bg0|3bg0]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC13, D3S1231E, SEC13L1, SEC13R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), NUP145, RAT10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC13, D3S1231E, SEC13L1, SEC13R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), NUP145, RAT10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bg1 OCA], [http://pdbe.org/3bg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bg1 RCSB], [http://www.ebi.ac.uk/pdbsum/3bg1 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bg1 OCA], [http://pdbe.org/3bg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bg1 RCSB], [http://www.ebi.ac.uk/pdbsum/3bg1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bg1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 13: Line 14:
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bg1_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bg1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 10:37, 31 October 2018

Architecture of a Coat for the Nuclear Pore MembraneArchitecture of a Coat for the Nuclear Pore Membrane

Structural highlights

3bg1 is a 8 chain structure with sequence from Atcc 18824 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:SEC13, D3S1231E, SEC13L1, SEC13R (HUMAN), NUP145, RAT10 (ATCC 18824)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SEC13_HUMAN] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles.[1] [NU145_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization.[2] [3] [4] [5] [6] [7] [8] [9] [10]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The symmetric core of the nuclear pore complex can be considered schematically as a series of concentric cylinders. A peripheral cylinder coating the pore membrane contains the previously characterized, elongated heptamer that harbors Sec13-Nup145C in its middle section. Strikingly, Sec13-Nup145C crystallizes as a hetero-octamer in two space groups. Oligomerization of Sec13-Nup145C was confirmed biochemically. Importantly, the numerous interacting surfaces in the hetero-octamer are evolutionarily highly conserved, further underlining the physiological relevance of the oligomerization. The hetero-octamer forms a slightly curved, yet rigid rod of sufficient length to span the entire height of the proposed membrane-adjacent cylinder. In concordance with the dimensions and symmetry of the nuclear pore complex core, we suggest that the cylinder is constructed of four antiparallel rings, each ring being composed of eight heptamers arranged in a head-to-tail fashion. Our model proposes that the hetero-octamer would vertically traverse and connect the four stacked rings.

Architecture of a coat for the nuclear pore membrane.,Hsia KC, Stavropoulos P, Blobel G, Hoelz A Cell. 2007 Dec 28;131(7):1313-26. PMID:18160040[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Tang BL, Peter F, Krijnse-Locker J, Low SH, Griffiths G, Hong W. The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol Cell Biol. 1997 Jan;17(1):256-66. PMID:8972206
  2. Fabre E, Boelens WC, Wimmer C, Mattaj IW, Hurt EC. Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell. 1994 Jul 29;78(2):275-89. PMID:8044840
  3. Wente SR, Blobel G. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J Cell Biol. 1994 Jun;125(5):955-69. PMID:8195299
  4. Sharma K, Fabre E, Tekotte H, Hurt EC, Tollervey D. Yeast nucleoporin mutants are defective in pre-tRNA splicing. Mol Cell Biol. 1996 Jan;16(1):294-301. PMID:8524308
  5. Teixeira MT, Siniossoglou S, Podtelejnikov S, Benichou JC, Mann M, Dujon B, Hurt E, Fabre E. Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins. EMBO J. 1997 Aug 15;16(16):5086-97. PMID:9305650 doi:10.1093/emboj/16.16.5086
  6. Teixeira MT, Fabre E, Dujon B. Self-catalyzed cleavage of the yeast nucleoporin Nup145p precursor. J Biol Chem. 1999 Nov 5;274(45):32439-44. PMID:10542288
  7. Galy V, Olivo-Marin JC, Scherthan H, Doye V, Rascalou N, Nehrbass U. Nuclear pore complexes in the organization of silent telomeric chromatin. Nature. 2000 Jan 6;403(6765):108-12. PMID:10638763 doi:10.1038/47528
  8. Lutzmann M, Kunze R, Buerer A, Aebi U, Hurt E. Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J. 2002 Feb 1;21(3):387-97. PMID:11823431 doi:10.1093/emboj/21.3.387
  9. Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2450-5. Epub 2003 Feb 25. PMID:12604785 doi:10.1073/pnas.0437902100
  10. Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol. 2004 Mar;6(3):197-206. Epub 2004 Feb 22. PMID:15039779 doi:10.1038/ncb1097
  11. Hsia KC, Stavropoulos P, Blobel G, Hoelz A. Architecture of a coat for the nuclear pore membrane. Cell. 2007 Dec 28;131(7):1313-26. PMID:18160040 doi:10.1016/j.cell.2007.11.038

3bg1, resolution 3.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA