This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1f3z

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 02:53, 11 September 2015

IIAGLC-ZN COMPLEX

Structural highlights

1f3z is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PTGA_ECOLI] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.

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

In Escherichia coli, the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS), IIAGlc (IIIGlc in older literature), is also the central regulatory protein of the PTS. Depending upon its state of phosphorylation, IIAGlc binds to a number of different proteins that display no apparent sequence homology. Previous structural studies suggested that nonspecific hydrophobic interactions, specific salt bridges, and an intermolecular Zn(II) binding site contribute to the wide latitude in IIAGlc binding sites. Two new crystal forms of IIAGlc have been solved at high resolution, and the models were compared to those previously studied. The major intermolecular contacts in the crystals differ in detail, but all involve the hydrophobic active site of IIAGlc interacting with a hydrophobic patch on a neighbor and all are shown to be surprisingly similar to the physiologically relevant regulatory interaction of IIAGlc with glycerol kinase. In two crystal forms, a helix on one molecule interacts with the face of another, while in the other crystal form, the primary crystal contact consists of a strand of beta-sheet that contributes to an intermolecular Zn(II) binding site with tetrahedral ligation identical to that of the zinc peptidase thermolysin. Thus, relatively nonspecific hydrophobic interactions combined with specific salt bridges and an intermolecular cation binding site (cation-promoted association) permit a regulatory protein to bind to target proteins that have little or no sequence or structural homology with one another. It is suggested that signal transduction by IIAGlc is a binary switch in which phosphorylation at the active site directly controls binding to target molecules.

Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition.,Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042^[1]

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

References

↑ Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ. Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition. Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042 doi:10.1021/bi971999e

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/1f3z"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></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=1f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f3z RCSB], [http://www.ebi.ac.uk/pdbsum/1f3z PDBsum]</span></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=1f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3z OCA], [http://pdbe.org/1f3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f3z RCSB], [http://www.ebi.ac.uk/pdbsum/1f3z PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1f3z" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1f3z

From Proteopedia

Revision as of 02:53, 11 September 2015

IIAGLC-ZN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox