1rc2

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[[Image:1rc2.gif|left|200px]]
 
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{{Structure
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==2.5 Angstrom Resolution X-ray Structure of Aquaporin Z==
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|PDB= 1rc2 |SIZE=350|CAPTION= <scene name='initialview01'>1rc2</scene>, resolution 2.5&Aring;
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<StructureSection load='1rc2' size='340' side='right'caption='[[1rc2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>
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<table><tr><td colspan='2'>[[1rc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RC2 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.5&#8491;</td></tr>
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|GENE= AQPZ, BNIP, B0875, C1009, SF0832, S0873 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene></td></tr>
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|DOMAIN=
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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=1rc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rc2 OCA], [https://pdbe.org/1rc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1rc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rc2 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rc2 OCA], [http://www.ebi.ac.uk/pdbsum/1rc2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rc2 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AQPZ_ECOLI AQPZ_ECOLI] Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.<ref>PMID:10400575</ref> <ref>PMID:10518952</ref> <ref>PMID:11493683</ref>
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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/rc/1rc2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1rc2 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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Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.
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'''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z'''
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Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z.,Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. PMID:14691544<ref>PMID:14691544</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 1rc2" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.
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*[[Aquaporin 3D structures|Aquaporin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1RC2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z., Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM, PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14691544 14691544]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Egea, P F.]]
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[[Category: Egea PF]]
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[[Category: III, J D.O Connell.]]
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[[Category: O'Connell III JD]]
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[[Category: Robles, Y C.]]
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[[Category: Robles YC]]
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[[Category: Savage, D F.]]
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[[Category: Savage DF]]
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[[Category: Stroud, R M.]]
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[[Category: Stroud RM]]
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[[Category: aquaporin]]
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[[Category: membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:26:04 2008''
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Current revision

2.5 Angstrom Resolution X-ray Structure of Aquaporin Z

PDB ID 1rc2

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