1mi1: Difference between revisions

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<StructureSection load='1mi1' size='340' side='right'caption='[[1mi1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1mi1' size='340' side='right'caption='[[1mi1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mi1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mi1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI1 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [https://pdbe.org/1mi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi1 ProSAT], [https://www.topsan.org/Proteins/NESGC/1mi1 TOPSAN]</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=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [https://pdbe.org/1mi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi1 ProSAT], [https://www.topsan.org/Proteins/NESGC/1mi1 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NBEA_HUMAN NBEA_HUMAN]] Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).[UniProtKB:Q9EPN1]  
[https://www.uniprot.org/uniprot/NBEA_HUMAN NBEA_HUMAN] Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).[UniProtKB:Q9EPN1]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mi1 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mi1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.
Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.,Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919<ref>PMID:12234919</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mi1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gebauer, D]]
[[Category: Gebauer D]]
[[Category: Jogl, G]]
[[Category: Jogl G]]
[[Category: Kashkar, H]]
[[Category: Kashkar H]]
[[Category: Kroenke, M]]
[[Category: Kroenke M]]
[[Category: Li, J]]
[[Category: Li J]]
[[Category: Structural genomic]]
[[Category: Shen Y]]
[[Category: Shen, Y]]
[[Category: Tong L]]
[[Category: Tong, L]]
[[Category: Wiegmann K]]
[[Category: Wiegmann, K]]
[[Category: Beach domain]]
[[Category: Nesg]]
[[Category: Ph domain]]
[[Category: PSI, Protein structure initiative]]
[[Category: Signal transduction]]
[[Category: Signaling protein]]
[[Category: Vesicle trafficking]]

Revision as of 08:36, 10 April 2024

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

1mi1, resolution 2.90Å

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