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1bg5

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CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE

Structural highlights

1bg5 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GST26_SCHJA Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

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 ankyrin 33-residue repeating motif, an L-shaped structure with protruding beta-hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and alpha-Na,K-ATPase, a ubiquitous membrane protein critical to vectorial transport of ions and nutrients, is required to assemble and stabilize Na,K-ATPase at the plasma membrane. alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (AnkG, a product of the ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its second cytoplasmic domain. Fusion peptides of glutathione S-transferase incorporating these 25 amino acids bind specifically to purified ankyrin (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double beta-strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests that the valency and specificity of ankyrin binding is achieved by the interaction of 5-7-residue surface loops with the beta-hairpin tips of multiple ankyrin repeat units.

Structure of the ankyrin-binding domain of alpha-Na,K-ATPase.,Zhang Z, Devarajan P, Dorfman AL, Morrow JS J Biol Chem. 1998 Jul 24;273(30):18681-4. PMID:9668035^[1]

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

References

↑ Zhang Z, Devarajan P, Dorfman AL, Morrow JS. Structure of the ankyrin-binding domain of alpha-Na,K-ATPase. J Biol Chem. 1998 Jul 24;273(30):18681-4. PMID:9668035

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bg5"

Categories: Large Structures | Rattus norvegicus | Devarajan P | Morrow JS | Zhang Z

@@ Line 3: / Line 3: @@
 <StructureSection load='1bg5' size='340' side='right'caption='[[1bg5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bg5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BG5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bg5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BG5 FirstGlance]. <br>
-</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=1bg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg5 OCA], [https://pdbe.org/1bg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg5 ProSAT]</span></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]] 2.6&#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=1bg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg5 OCA], [https://pdbe.org/1bg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
+[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Devarajan, P]]
+[[Category: Rattus norvegicus]]
-[[Category: Morrow, J S]]
+[[Category: Devarajan P]]
-[[Category: Zhang, Z]]
+[[Category: Morrow JS]]
-[[Category: Ankyrin binding]]
+[[Category: Zhang Z]]
-[[Category: Atpase]]
-[[Category: Carrier crystallization]]
-[[Category: Glutathione-s-transferase]]
-[[Category: Ion transport]]

1bg5

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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