2hid: Difference between revisions

No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS==
==REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS==
<StructureSection load='2hid' size='340' side='right' caption='[[2hid]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='2hid' size='340' side='right'caption='[[2hid]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hid 1hid]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HID FirstGlance]. <br>
<table><tr><td colspan='2'>[[2hid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hid 1hid]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HID FirstGlance]. <br>
</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=2hid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hid OCA], [http://pdbe.org/2hid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hid RCSB], [http://www.ebi.ac.uk/pdbsum/2hid PDBsum]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=2hid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hid OCA], [https://pdbe.org/2hid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hid RCSB], [https://www.ebi.ac.uk/pdbsum/2hid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hid ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PTHP_BACSU PTHP_BACSU]] 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).<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>  P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>
[https://www.uniprot.org/uniprot/PTHP_BACSU PTHP_BACSU] 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).<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>  P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/2hid_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/2hid_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2hid ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 28: Line 30:


==See Also==
==See Also==
*[[Phosphocarrier protein HPr|Phosphocarrier protein HPr]]
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus globigii migula 1900]]
[[Category: Bacillus subtilis]]
[[Category: Jones, B E]]
[[Category: Large Structures]]
[[Category: Klevit, R E]]
[[Category: Jones BE]]
[[Category: Rajagopal, P]]
[[Category: Klevit RE]]
[[Category: Histidine containing protein]]
[[Category: Rajagopal P]]
[[Category: Phosphotransferase]]
[[Category: Pt]]

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

OCA