2hid

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hid]] is a 1 chain structure with sequence from [http://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 [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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HID FirstGlance]. <br>
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</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=2hid RCSB], [http://www.ebi.ac.uk/pdbsum/2hid PDBsum]</span></td></tr>
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</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://www.rcsb.org/pdb/explore.do?structureId=2hid RCSB], [http://www.ebi.ac.uk/pdbsum/2hid PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Jones, B E.]]
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[[Category: Jones, B E]]
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[[Category: Klevit, R E.]]
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[[Category: Klevit, R E]]
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[[Category: Rajagopal, P.]]
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[[Category: Rajagopal, P]]
[[Category: Histidine containing protein]]
[[Category: Histidine containing protein]]
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
[[Category: Pt]]
[[Category: Pt]]

Revision as of 22:16, 25 December 2014

REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS

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