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4r0y

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Structure of Maltose-binding Protein Fusion with the C-terminal GH1 domain of Guanylate Kinase-associated Protein from Rattus norvegicus

Structural highlights

4r0y is a 2 chain structure with sequence from Escherichia coli K-12 and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.DLGP1_RAT Part of the postsynaptic scaffold in neuronal cells.

Publication Abstract from PubMed

Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank-Homer complexes by protein-protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0A resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix alpha4 which was not visible in the crystal structure associates weakly with the helix alpha3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein-protein interaction module for the synaptic protein clustering.

Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus.,Tong J, Yang H, Eom SH, Chun C, Im YJ Biochem Biophys Res Commun. 2014 Aug 22. pii: S0006-291X(14)01496-X. doi:, 10.1016/j.bbrc.2014.08.073. PMID:25152391^[1]

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

References

↑ Tong J, Yang H, Eom SH, Chun C, Im YJ. Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus. Biochem Biophys Res Commun. 2014 Aug 22. pii: S0006-291X(14)01496-X. doi:, 10.1016/j.bbrc.2014.08.073. PMID:25152391 doi:http://dx.doi.org/10.1016/j.bbrc.2014.08.073

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r0y"

Categories: Escherichia coli K-12 | Large Structures | Rattus norvegicus | Im YJ | Tong J

@@ Line 1: / Line 1: @@
 ==Structure of Maltose-binding Protein Fusion with the C-terminal GH1 domain of Guanylate Kinase-associated Protein from Rattus norvegicus==
-<StructureSection load='4r0y' size='340' side='right' caption='[[4r0y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4r0y' size='340' side='right'caption='[[4r0y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4r0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4r0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R0Y FirstGlance]. <br>
-</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=4r0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0y OCA], [http://pdbe.org/4r0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0y RCSB], [http://www.ebi.ac.uk/pdbsum/4r0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0y 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&#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=4r0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0y OCA], [https://pdbe.org/4r0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r0y RCSB], [https://www.ebi.ac.uk/pdbsum/4r0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/DLGP1_RAT DLGP1_RAT] Part of the postsynaptic scaffold in neuronal cells.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Escherichia coli K-12]]
-[[Category: Im, Y J]]
+[[Category: Large Structures]]
-[[Category: Tong, J]]
+[[Category: Rattus norvegicus]]
-[[Category: Protein binding]]
+[[Category: Im YJ]]
-[[Category: Synaptic scaffolding protein]]
+[[Category: Tong J]]
-[[Category: Three-helix bundle]]

4r0y

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Current revision

Structure of Maltose-binding Protein Fusion with the C-terminal GH1 domain of Guanylate Kinase-associated Protein from Rattus norvegicus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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