1w24: Difference between revisions

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OCA

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-[[Image:1w24.gif|left|200px]]<br />
-<applet load="1w24" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1w24, resolution 2.10&Aring;" />
-'''CRYSTAL STRUCTURE OF HUMAN VPS29'''<br />
-==Overview==
+==Crystal Structure Of human Vps29==
-Vacuolar protein sorting protein 29 (Vps29p), which is involved in, retrograde trafficking from prevacuolar endosomes to the trans-Golgi, network, performs its biological functions by participating in the, formation of a "retromer complex." In human cells, this complex comprises, four conserved proteins: hVps35p, hVps29p, hVps26p, and sorting nexin 1, protein (SNX1). Here, we report the crystal structure of hVps29p at 2.1, Angstroms resolution, the first three-dimensional structure of the, retromer subunits. This novel structure adopts a four-layered, alpha-beta-beta-alpha sandwich fold. hVps29p contains a metal-binding site, that is very similar to the active sites of some proteins of the, phosphodiesterase/nuclease protein family, indicating that hVps29p may, carry out chemically similar functions. Structure and sequence, conservation analysis suggests that hVps29p contains two protein-protein, interaction sites. One site, which potentially serves as the interface, between hVps29p and hVps35p, comprises 5 conserved hydrophobic and 8, hydrophilic residues. The other site is relatively more hydrophilic and, may serve as a binding interface with hVps26p, SNX1, or other target, proteins.
+<StructureSection load='1w24' size='340' side='right'caption='[[1w24]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1w24]] is a 1 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=1W24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W24 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=1w24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w24 OCA], [https://pdbe.org/1w24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w24 RCSB], [https://www.ebi.ac.uk/pdbsum/1w24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w24 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VPS29_HUMAN VPS29_HUMAN] Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Has low protein phosphatase activity towards a serine-phosphorylated peptide derived from IGF2R (in vitro).<ref>PMID:15247922</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w2/1w24_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1w24 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Vacuolar protein sorting protein 29 (Vps29p), which is involved in retrograde trafficking from prevacuolar endosomes to the trans-Golgi network, performs its biological functions by participating in the formation of a "retromer complex." In human cells, this complex comprises four conserved proteins: hVps35p, hVps29p, hVps26p, and sorting nexin 1 protein (SNX1). Here, we report the crystal structure of hVps29p at 2.1 Angstroms resolution, the first three-dimensional structure of the retromer subunits. This novel structure adopts a four-layered alpha-beta-beta-alpha sandwich fold. hVps29p contains a metal-binding site that is very similar to the active sites of some proteins of the phosphodiesterase/nuclease protein family, indicating that hVps29p may carry out chemically similar functions. Structure and sequence conservation analysis suggests that hVps29p contains two protein-protein interaction sites. One site, which potentially serves as the interface between hVps29p and hVps35p, comprises 5 conserved hydrophobic and 8 hydrophilic residues. The other site is relatively more hydrophilic and may serve as a binding interface with hVps26p, SNX1, or other target proteins.
-==About this Structure==
+Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites.,Wang D, Guo M, Liang Z, Fan J, Zhu Z, Zang J, Zhu Z, Li X, Teng M, Niu L, Dong Y, Liu P J Biol Chem. 2005 Jun 17;280(24):22962-7. Epub 2005 Mar 23. PMID:15788412<ref>PMID:15788412</ref>
-W24 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=1W24 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites., Wang D, Guo M, Liang Z, Fan J, Zhu Z, Zang J, Zhu Z, Li X, Teng M, Niu L, Dong Y, Liu P, J Biol Chem. 2005 Jun 17;280(24):22962-7. Epub 2005 Mar 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15788412 15788412]
+</div>
+<div class="pdbe-citations 1w24" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Guo, M.]]
+[[Category: Guo M]]
-[[Category: Niu, L.]]
+[[Category: Niu L]]
-[[Category: Teng, M.]]
+[[Category: Teng M]]
-[[Category: Wang, D.]]
+[[Category: Wang D]]
-[[Category: alpha-beta-beta-alpha sandwich]]
-[[Category: vacuolar protein sorting protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:46:11 2007''