2lbf: Difference between revisions

← Older edit Newer edit →

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2lbf.jpg|left|200px]]
+==Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer==
+<StructureSection load='2lbf' size='340' side='right' caption='[[2lbf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+== Structural highlights ==
+[[2lbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBF OCA]. <br>
+<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+== Publication Abstract from PubMed ==
+The lateral ribosomal stalk is responsible for the kingdom-specific binding of translation factors and activation of GTP hydrolysis during protein synthesis. The eukaryotic stalk is composed of three acidic ribosomal proteins P0, P1 and P2. P0 binds two copies of P1/P2 hetero-dimers to form a pentameric P-complex. The structure of the eukaryotic stalk is currently not known. To provide a better understanding on the structural organization of eukaryotic stalk, we have determined the solution structure of the N-terminal dimerization domain (NTD) of P1/P2 hetero-dimer. Helix-1, -2 and -4 from each of the NTD-P1 and NTD-P2 form the dimeric interface that buries 2200 A(2) of solvent accessible surface area. In contrast to the symmetric P2 homo-dimer, P1/P2 hetero-dimer is asymmetric. Three conserved hydrophobic residues on the surface of NTD-P1 are replaced by charged residues in NTD-P2. Moreover, NTD-P1 has an extra turn in helix-1, which forms extensive intermolecular interactions with helix-1 and -4 of NTD-P2. Truncation of this extra turn of P1 abolished the formation of P1/P2 hetero-dimer. Systematic truncation studies suggest that P0 contains two spine-helices that each binds one copy of P1/P2 hetero-dimer. Modeling studies suggest that a large hydrophobic cavity, which can accommodate the loop between the spine-helices of P0, can be found on NTD-P1 but not on NTD-P2 when the helix-4 adopts an 'open' conformation. Based on the asymmetric properties of NTD-P1/NTD-P2, a structural model of the eukaryotic P-complex with P2/P1:P1/P2 topology is proposed.
-<!--
+Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex.,Lee KM, Yu CW, Chiu TY, Sze KH, Shaw PC, Wong KB Nucleic Acids Res. 2011 Dec 1. PMID:22135285<ref>PMID:22135285</ref>
-The line below this paragraph, containing "STRUCTURE_2lbf", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2lbf|  PDB=2lbf  |  SCENE=  }}
-===Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+== References ==
+<references/>
-<!--
+__TOC__
-The line below this paragraph, {{ABSTRACT_PUBMED_22135285}}, adds the Publication Abstract to the page
+</StructureSection>
-(as it appears on PubMed at http://www.pubmed.gov), where 22135285 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_22135285}}
-==About this Structure==
-[[2lbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBF OCA].
-==Reference==
-<ref group="xtra">PMID:022135285</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
 [[Category: Chiu, T Y.H.]]