1sph: Difference between revisions

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New page: left|200px<br /><applet load="1sph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sph, resolution 2.0Å" /> '''REFINED STRUCTURES OF...
 
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[[Image:1sph.gif|left|200px]]<br /><applet load="1sph" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sph, resolution 2.0&Aring;" />
'''REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION'''<br />


==Overview==
==REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION==
BACKGROUND: The histidine-containing phosphocarrier protein (HPr), functions in the bacterial phosphoenolpyruvate:sugar phosphotransferase, system (PTS). His15 on HPr accepts a phosphoryl group from Enzyme I and, transfers it to the Enzyme IIA domain of a sugar-specific PTS permease. In, addition, HPrs from Gram-positive bacteria undergo phosphorylation on a, serine residue, Ser46, which inhibits phosphorylation at His15 and sugar, transport. The questions to be addressed at the molecular level are: what, is the mechanism of each of the phosphoryl transfers and what, conformational transitions are associated with each event? RESULTS: Thus, the crystal structures of the mutants Ser83--&gt;Cys HPr (fully active, protein) and Ser46--&gt;Asp HPr (impaired protein which mimics Ser46, approximately P HPr) from Bacillus subtilis have been determined at 2 A, resolution. They have been crystallized from high-salt and low-salt, solutions respectively, and in two different space groups. Analysis of the, two crystal forms reveals some significant differences but these do not, alter the overall fold of the protein. In each structure, the side chain, of His15 caps the following helix. Two alternative side-chain, conformations of Arg17 are observed; it either forms an ion pair with a, sulfate ion, presumably resembling the phosphorylated state of the protein, (high-salt crystal) or with Glu84 (low-salt crystal). The main-chain, conformation in the region of residue 46 is the same in the two crystal, forms, with both Ser46 and Asp46 capping the following helix. CONCLUSIONS:, The analysis suggests that phosphorylation of either His15 or Ser46 is not, associated with main-chain conformational transitions. Rather, the protein, is poised to accept the respective phosphoryl group with minor adjustments, to side chains. The inhibitory effect of phosphorylation on Ser46 is, attributed to the altered surface electrostatics, which impairs, protein-protein interaction.
<StructureSection load='1sph' size='340' side='right'caption='[[1sph]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sph]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#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=1sph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sph OCA], [https://pdbe.org/1sph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sph RCSB], [https://www.ebi.ac.uk/pdbsum/1sph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sph ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
[[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/sp/1sph_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=1sph ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SPH OCA].
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 
== References ==
==Reference==
<references/>
Refined structures of the active Ser83--&gt;Cys and impaired Ser46--&gt;Asp histidine-containing phosphocarrier proteins., Liao DI, Herzberg O, Structure. 1994 Dec 15;2(12):1203-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7704530 7704530]
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Herzberg, O.]]
[[Category: Herzberg O]]
[[Category: Liao, D.I.]]
[[Category: Liao D-I]]
[[Category: phosphotransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:32:50 2007''

Latest revision as of 11:32, 14 February 2024

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITIONREFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

Structural highlights

1sph is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] 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.[3] [4]

Evolutionary Conservation

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

See Also

References

  1. ↑ Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH Jr, Steinmetz M. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol. 1994 Jun;176(11):3336-44. PMID:8195089
  2. ↑ Fujita Y, Miwa Y, Galinier A, Deutscher J. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol Microbiol. 1995 Sep;17(5):953-60. PMID:8596444
  3. ↑ Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH Jr, Steinmetz M. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol. 1994 Jun;176(11):3336-44. PMID:8195089
  4. ↑ Fujita Y, Miwa Y, Galinier A, Deutscher J. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol Microbiol. 1995 Sep;17(5):953-60. PMID:8596444

1sph, resolution 2.00Å

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