2o9d

From Proteopedia

(Difference between revisions)

Revision as of 12:50, 9 June 2021

Crystal Structure of AqpZ mutant T183C.

Structural highlights

2o9d is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2o9e, 2o9f, 2o9g
Gene:	aqpZ, bniP ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The aquaporin family of channels was defined based on the inhibition of water transport by mercurial compounds. Despite the important role of mercurials, little is known about the structural changes involved upon mercury binding leading to channel inhibition. To elucidate the mechanism we designed a mutant, T183C, of aquaporin Z (AqpZ) patterned after the known mercury-sensitive site of aquaporin 1 (AQP1) and determined the X-ray crystal structures of the unbound and mercury blocked states. Superposition of the two structures shows no conformational rearrangement upon mercury binding. In the blocked structure, there are two mercury sites, one bound to Cys183 and occluding the pore, and a second, also bound to the same cysteine but found buried in an interstitial cavity. To test the mechanism of blockade we designed a different mutant, L170C, to produce a more effective mercury block at the pore site. In a dose-response inhibition study, this mutant was 20 times more sensitive to mercury than wild-type AqpZ and four times more sensitive than T183C. The X-ray structure of L170C shows four mercury atoms at, or near, the pore site defined in the T183C structure and no structural change upon mercury binding. Thus, we elucidate a steric inhibition mechanism for this important class of channels by mercury.

Structural basis of aquaporin inhibition by mercury.,Savage DF, Stroud RM J Mol Biol. 2007 May 4;368(3):607-17. Epub 2007 Mar 2. PMID:17376483^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Delamarche C, Thomas D, Rolland JP, Froger A, Gouranton J, Svelto M, Agre P, Calamita G. Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy. J Bacteriol. 1999 Jul;181(14):4193-7. PMID:10400575
↑ Borgnia MJ, Kozono D, Calamita G, Maloney PC, Agre P. Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol. 1999 Sep 3;291(5):1169-79. PMID:10518952 doi:http://dx.doi.org/S0022-2836(99)93032-2
↑ Pohl P, Saparov SM, Borgnia MJ, Agre P. Highly selective water channel activity measured by voltage clamp: analysis of planar lipid bilayers reconstituted with purified AqpZ. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9624-9. Epub 2001 Aug 7. PMID:11493683 doi:http://dx.doi.org/10.1073/pnas.161299398
↑ Savage DF, Stroud RM. Structural basis of aquaporin inhibition by mercury. J Mol Biol. 2007 May 4;368(3):607-17. Epub 2007 Mar 2. PMID:17376483 doi:10.1016/j.jmb.2007.02.070

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o9d"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of AqpZ mutant T183C.==
-<StructureSection load='2o9d' size='340' side='right' caption='[[2o9d]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='2o9d' size='340' side='right'caption='[[2o9d]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2o9d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O9D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2o9d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O9D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSG:OCTYL+ALPHA-L-ALTROPYRANOSIDE'>HSG</scene>, <scene name='pdbligand=HSH:OCTYL+BETA-D-GALACTOPYRANOSIDE'>HSH</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSG:OCTYL+ALPHA-L-ALTROPYRANOSIDE'>HSG</scene>, <scene name='pdbligand=HSH:OCTYL+BETA-D-GALACTOPYRANOSIDE'>HSH</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o9e|2o9e]], [[2o9f|2o9f]], [[2o9g|2o9g]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2o9e|2o9e]], [[2o9f|2o9f]], [[2o9g|2o9g]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aqpZ, bniP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aqpZ, bniP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<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=2o9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9d OCA], [http://pdbe.org/2o9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o9d RCSB], [http://www.ebi.ac.uk/pdbsum/2o9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o9d ProSAT]</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=2o9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9d OCA], [https://pdbe.org/2o9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o9d RCSB], [https://www.ebi.ac.uk/pdbsum/2o9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o9d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Aquaporin|Aquaporin]]
+*[[Aquaporin 3D structures|Aquaporin 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: CSMP, Center for Structures of Membrane Proteins]]
 [[Category: Savage, D F]]

2o9d

From Proteopedia

Revision as of 12:50, 9 June 2021

Crystal Structure of AqpZ mutant T183C.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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