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1ezp

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GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-CYCLODEXTRIN USING PEPTIDE ORIENTATIONS FROM DIPOLAR COUPLINGS

Structural highlights

1ezp 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

The global fold of maltose-binding protein in complex with the substrate beta-cyclodextrin was determined by solution NMR methods. The two-domain protein is comprised of a single polypeptide chain of 370 residues, with a molecular mass of 42 kDa. Distance information in the form of H(N)-H(N), H(N)-CH(3) and CH(3)-CH(3) NOEs was recorded on (15)N, (2)H and (15)N, (13)C, (2)H-labeled proteins with methyl protonation in Val, Leu, and Ile (C(delta1) only) residues. Distances to methyl protons, critical for the structure determination, comprised 77 % of the long-range restraints. Initial structures were calculated on the basis of 1943 NOEs, 48 hydrogen bond and 555 dihedral angle restraints. A global pair-wise backbone rmsd of 5.5 A was obtained for these initial structures with rmsd values for the N and C domains of 2.4 and 3.8 A, respectively. Direct refinement against one-bond (1)H(N)-(15)N, (13)C(alpha)-(13)CO, (15)N-(13)CO, two-bond (1)H(N)-(13)CO and three-bond (1)H(N)-(13)C(alpha) dipolar couplings resulted in structures with large numbers of dipolar restraint violations. As an alternative to direct refinement against measured dipolar couplings we have developed an approach where discrete orientations are calculated for each peptide plane on the basis of the dipolar couplings described above. The orientation which best matches that in initial NMR structures calculated from NOE and dihedral angle restraints exclusively is used to refine further the structures using a new module written for CNS. Modeling studies from four different proteins with diverse structural motifs establishes the utility of the methodology. When applied to experimental data recorded on MBP the precision of the family of structures generated improves from 5.5 to 2.2 A, while the rmsd with respect to the X-ray structure (1dmb) is reduced from 5.1 to 3.3 A.

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein.,Mueller GA, Choy WY, Yang D, Forman-Kay JD, Venters RA, Kay LE J Mol Biol. 2000 Jun 30;300(1):197-212. PMID:10864509^[1]

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

References

↑ Mueller GA, Choy WY, Yang D, Forman-Kay JD, Venters RA, Kay LE. Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein. J Mol Biol. 2000 Jun 30;300(1):197-212. PMID:10864509 doi:10.1006/jmbi.2000.3842

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/1ezp"

@@ Line 1: / Line 1: @@
 ==GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-CYCLODEXTRIN USING PEPTIDE ORIENTATIONS FROM DIPOLAR COUPLINGS==
-<StructureSection load='1ezp' size='340' side='right'caption='[[1ezp]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1ezp' size='340' side='right'caption='[[1ezp]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ezp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EZP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ezp]] 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=1EZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EZP FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ezo|1ezo]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ezp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezp OCA], [http://pdbe.org/1ezp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ezp RCSB], [http://www.ebi.ac.uk/pdbsum/1ezp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ezp 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=1ezp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezp OCA], [https://pdbe.org/1ezp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ezp RCSB], [https://www.ebi.ac.uk/pdbsum/1ezp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ezp 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 30: / 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: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Choy, W Y]]
+[[Category: Choy WY]]
-[[Category: Forman-Kay, J D]]
+[[Category: Forman-Kay JD]]
-[[Category: Kay, L E]]
+[[Category: Kay LE]]
-[[Category: Mueller, G A]]
+[[Category: Mueller GA]]
-[[Category: Venters, R A]]
+[[Category: Venters RA]]
-[[Category: Yang, D]]
+[[Category: Yang D]]
-[[Category: Deuteration]]
-[[Category: Methyl labeling]]
-[[Category: Residual diplar coupling]]
-[[Category: Sugar binding protein]]

1ezp

From Proteopedia

Current revision

GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-CYCLODEXTRIN USING PEPTIDE ORIENTATIONS FROM DIPOLAR COUPLINGS

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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