1ola

From Proteopedia

(Difference between revisions)

Revision as of 07:14, 25 August 2021

THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA

Structural highlights

1ola is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OPPA_SALTY] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.

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

Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.

The structural basis of sequence-independent peptide binding by OppA protein.,Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ Science. 1994 Jun 10;264(5165):1578-81. PMID:8202710^[1]

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

References

↑ Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ. The structural basis of sequence-independent peptide binding by OppA protein. Science. 1994 Jun 10;264(5165):1578-81. PMID:8202710

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/1ola"

Categories: Large Structures | Tame, J | Wilkinson, A J | Binding protein

@@ Line 3: / Line 3: @@
 <StructureSection load='1ola' size='340' side='right'caption='[[1ola]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ola]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OLA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ola]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></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=1ola FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ola OCA], [http://pdbe.org/1ola PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ola RCSB], [http://www.ebi.ac.uk/pdbsum/1ola PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ola 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=1ola FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ola OCA], [https://pdbe.org/1ola PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ola RCSB], [https://www.ebi.ac.uk/pdbsum/1ola PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ola ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OPPA_SALTY OPPA_SALTY]] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.
+[[https://www.uniprot.org/uniprot/OPPA_SALTY OPPA_SALTY]] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Oligopeptide-binding protein|Oligopeptide-binding protein]]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
 == References ==
 <references/>

1ola

From Proteopedia

Revision as of 07:14, 25 August 2021

THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA

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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