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2h25

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Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin

Structural highlights

2h25 is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
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.

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

So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins <30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling.

A new strategy for structure determination of large proteins in solution without deuteration.,Xu Y, Zheng Y, Fan JS, Yang D Nat Methods. 2006 Nov;3(11):931-7. PMID:17060917^[1]

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

References

↑ Xu Y, Zheng Y, Fan JS, Yang D. A new strategy for structure determination of large proteins in solution without deuteration. Nat Methods. 2006 Nov;3(11):931-7. PMID:17060917 doi:10.1038/nmeth938

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/2h25"

@@ Line 1: / Line 1: @@
 ==Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin==
-<StructureSection load='2h25' size='340' side='right' caption='[[2h25]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2h25' size='340' side='right'caption='[[2h25]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2h25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H25 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H25 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=2h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h25 OCA], [http://pdbe.org/2h25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h25 RCSB], [http://www.ebi.ac.uk/pdbsum/2h25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h25 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h25 OCA], [https://pdbe.org/2h25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h25 RCSB], [https://www.ebi.ac.uk/pdbsum/2h25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h25 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 30: @@
 ==See Also==
-*[[Maltose-binding protein|Maltose-binding protein]]
+*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Lin, Z]]
+[[Category: Large Structures]]
-[[Category: Xu, Y]]
+[[Category: Lin Z]]
-[[Category: Yang, D]]
+[[Category: Xu Y]]
-[[Category: Zheng, Y]]
+[[Category: Yang D]]
-[[Category: Alpha/beta protein]]
+[[Category: Zheng Y]]
-[[Category: Sugar binding protein]]

2h25

From Proteopedia

Current revision

Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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