1mi1

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(New page: 200px<br /> <applet load="1mi1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mi1, resolution 2.90&Aring;" /> '''Crystal Structure o...)
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[[Image:1mi1.gif|left|200px]]<br />
 
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<applet load="1mi1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mi1, resolution 2.90&Aring;" />
 
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'''Crystal Structure of the PH-BEACH Domain of Human Neurobeachin'''<br />
 
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==Overview==
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==Crystal Structure of the PH-BEACH Domain of Human Neurobeachin==
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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.
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<StructureSection load='1mi1' size='340' side='right'caption='[[1mi1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.9&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/1mi1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1MI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12234919 12234919]
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</div>
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<div class="pdbe-citations 1mi1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gebauer, D.]]
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[[Category: Gebauer D]]
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[[Category: Jogl, G.]]
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[[Category: Jogl G]]
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[[Category: Kashkar, H.]]
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[[Category: Kashkar H]]
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[[Category: Kroenke, M.]]
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[[Category: Kroenke M]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
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[[Category: Shen Y]]
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[[Category: Shen, Y.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: Wiegmann K]]
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[[Category: Wiegmann, K.]]
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[[Category: beach domain]]
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[[Category: nesg]]
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[[Category: northeast structural genomics consortium]]
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[[Category: ph domain]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: signal transduction]]
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[[Category: structural genomics]]
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[[Category: vesicle trafficking]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:39 2007''
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Current revision

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

PDB ID 1mi1

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