4ht5: Difference between revisions

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==CO2 concentrating mechanism protein P, CcmP form 1==
==CO2 concentrating mechanism protein P, CcmP form 1==
<StructureSection load='4ht5' size='340' side='right' caption='[[4ht5]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='4ht5' size='340' side='right'caption='[[4ht5]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ht5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HT5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ht5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT5 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ht7|4ht7]]</td></tr>
</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=4ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht5 OCA], [https://pdbe.org/4ht5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht5 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">syc1000_c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269084 Anacystis nidulans])</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=4ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht5 OCA], [http://pdbe.org/4ht5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ht5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ht5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCMP_SYNE7 CCMP_SYNE7] Probably part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. It is thought that this protein controls transport of RuBisCO reactants in and out of the carboxysome; residual densities in the 4 X-ray structures suggest that differing compounds bind in interior pockets, depending on the open or closed state of the pore.<ref>PMID:23572529</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anacystis nidulans]]
[[Category: Large Structures]]
[[Category: Cai, F]]
[[Category: Synechococcus elongatus PCC 6301]]
[[Category: Kerfeld, C A]]
[[Category: Cai F]]
[[Category: Sutter, M]]
[[Category: Kerfeld CA]]
[[Category: Bmc]]
[[Category: Sutter M]]
[[Category: Carboxysome]]
[[Category: Protein binding]]
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