3eze

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:26, 28 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3eze.jpg|left|200px]]
 
-
{{Structure
+
==COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE==
-
|PDB= 3eze |SIZE=350|CAPTION= <scene name='initialview01'>3eze</scene>
+
<StructureSection load='3eze' size='340' side='right'caption='[[3eze]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>
+
<table><tr><td colspan='2'>[[3eze]] is a 2 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=3EZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EZE FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eze OCA], [https://pdbe.org/3eze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eze RCSB], [https://www.ebi.ac.uk/pdbsum/3eze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eze ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[3eza|3EZA]], [[3ezb|3EZB]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eze OCA], [http://www.ebi.ac.uk/pdbsum/3eze PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3eze RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/PT1_ECOLI PT1_ECOLI] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).<ref>PMID:7876255</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/3eze_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3eze ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.
-
'''COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE'''
+
Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.,Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Clore GM Nat Struct Biol. 1999 Feb;6(2):166-73. PMID:10048929<ref>PMID:10048929</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3eze" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.
+
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
3EZE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZE OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr., Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Clore GM, Nat Struct Biol. 1999 Feb;6(2):166-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10048929 10048929]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
+
[[Category: Large Structures]]
-
[[Category: Protein complex]]
+
[[Category: Clore GM]]
-
[[Category: Clore, G M.]]
+
[[Category: Garrett DS]]
-
[[Category: Garrett, D S.]]
+
[[Category: Gronenborn AM]]
-
[[Category: Gronenborn, A M.]]
+
-
[[Category: kinase]]
+
-
[[Category: phosphotransferase]]
+
-
[[Category: sugar transport]]
+
-
[[Category: transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:33:18 2008''
+

Current revision

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

PDB ID 3eze

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3eze"
Personal tools