1cm2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1cm2.png|left|200px]]


<!--
==STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.==
The line below this paragraph, containing "STRUCTURE_1cm2", creates the "Structure Box" on the page.
<StructureSection load='1cm2' size='340' side='right'caption='[[1cm2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1cm2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CM2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1cm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm2 OCA], [https://pdbe.org/1cm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cm2 ProSAT]</span></td></tr>
{{STRUCTURE_1cm2| PDB=1cm2 |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTHP_ECOLI PTHP_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. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).
== 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/cm/1cm2_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=1cm2 ConSurf].
<div style="clear:both"></div>


===STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.===
==See Also==
 
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 
__TOC__
<!--
</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_10419492}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10419492 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10419492}}
 
==About this Structure==
1CM2 is a [[Single protein]] structure of sequence 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=1CM2 OCA].
 
==Reference==
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization., Napper S, Delbaere LT, Waygood EB, J Biol Chem. 1999 Jul 30;274(31):21776-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10419492 10419492]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Delbaere, L T.J.]]
[[Category: Delbaere LTJ]]
[[Category: Napper, S.]]
[[Category: Napper S]]
[[Category: Waygood, E B.]]
[[Category: Waygood EB]]
[[Category: Isoimide]]
[[Category: Phosphotransferase]]
[[Category: Succinimide]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:56:06 2008''

Latest revision as of 08:57, 3 April 2024

STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.

Structural highlights

1cm2 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.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTHP_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. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1cm2, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA