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4fcc

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{{Large structure}}
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==Glutamate dehydrogenase from E. coli==
==Glutamate dehydrogenase from E. coli==
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<StructureSection load='4fcc' size='340' side='right' caption='[[4fcc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4fcc' size='340' side='right'caption='[[4fcc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fcc]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FCC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fcc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FCC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fhl|4fhl]], [[4fhm|4fhm]], [[4fhn|4fhn]]</td></tr>
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</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&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gdhA, ECs2467, Z2793 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fcc OCA], [https://pdbe.org/4fcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fcc RCSB], [https://www.ebi.ac.uk/pdbsum/4fcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fcc ProSAT]</span></td></tr>
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<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=4fcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fcc OCA], [http://pdbe.org/4fcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fcc RCSB], [http://www.ebi.ac.uk/pdbsum/4fcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fcc ProSAT]</span></td></tr>
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</table>
</table>
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{{Large structure}}
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/Q8XDW9_ECO57 Q8XDW9_ECO57]
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== Publication Abstract from PubMed ==
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Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of approximately 30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120-Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model.
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Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.,Bilokapic S, Schwartz TU Proc Natl Acad Sci U S A. 2012 Sep 18;109(38):15241-6. Epub 2012 Sep 5. PMID:22955883<ref>PMID:22955883</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fcc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Glutamate dehydrogenase|Glutamate dehydrogenase]]
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*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco57]]
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[[Category: Escherichia coli O157:H7]]
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[[Category: Bilokapic, S]]
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[[Category: Large Structures]]
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[[Category: Schwartz, T U]]
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[[Category: Bilokapic S]]
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[[Category: Metabolic role]]
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[[Category: Schwartz TU]]
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[[Category: Nad]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Protein complex]]
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[[Category: Rossmann fold]]
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Current revision

Glutamate dehydrogenase from E. coli

PDB ID 4fcc

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