2ygi: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ygi.png|left|200px]]
-<!--
+==Methanobactin HM1==
-The line below this paragraph, containing "STRUCTURE_2ygi", creates the "Structure Box" on the page.
+<StructureSection load='2ygi' size='340' side='right'caption='[[2ygi]], [[Resolution|resolution]] 0.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ygi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_hirsuta Methylocystis hirsuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGI FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HM7:3-METHYLTHIOETHANE-PYRAZINEDIONE'>HM7</scene>, <scene name='pdbligand=HM8:2-[(1S,2R)-1-AMINO-2-(SULFOOXY)PROPYL]-5-HYDROXY-1,3-OXAZOLE-4-CARBOTHIOIC+O-ACID'>HM8</scene></td></tr>
-{{STRUCTURE_2ygi|  PDB=2ygi  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ygi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygi OCA], [https://pdbe.org/2ygi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygi RCSB], [https://www.ebi.ac.uk/pdbsum/2ygi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygi ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Methane-oxidizing bacteria are nature's primary biological mechanism for suppressing atmospheric levels of the second-most important greenhouse gas via methane monooxygenases (MMOs). The copper-containing particulate enzyme is the most widespread and efficient MMO. Under low-copper conditions methane-oxidizing bacteria secrete the small copper-binding peptide methanobactin (mbtin) to acquire copper, but how variations in the structures of mbtins influence copper metabolism and species selection are unknown. Methanobactins have been isolated from Methylocystis strains M and hirsuta CSC1, organisms that can switch to using an iron-containing soluble MMO when copper is limiting, and the nonswitchover Methylocystis rosea. These mbtins are shorter, and have different amino acid compositions, than the characterized mbtin from Methylosinus trichosporium OB3b. A coordinating pyrazinedione ring in the Methylocystis mbtins has little influence on the Cu(I) site structure. The Methylocystis mbtins have a sulfate group that helps stabilize the Cu(I) forms, resulting in affinities of approximately 10(21) M(-1). The Cu(II) affinities vary over three orders of magnitude with reduction potentials covering approximately 250 mV, which may dictate the mechanism of intracellular copper release. Copper uptake and the switchover from using the iron-containing soluble MMO to the copper-containing particulate enzyme is faster when mediated by the native mbtin, suggesting that the amino acid sequence is important for the interaction of mbtins with receptors. The differences in structures and properties of mbtins, and their influence on copper utilization by methane-oxidizing bacteria, have important implications for the ecology and global function of these environmentally vital organisms.
-===Methanobactin HM1===
+Variations in methanobactin structure influences copper utilization by methane-oxidizing bacteria.,El Ghazouani A, Basle A, Gray J, Graham DW, Firbank SJ, Dennison C Proc Natl Acad Sci U S A. 2012 May 29;109(22):8400-4. Epub 2012 May 10. PMID:22582172<ref>PMID:22582172</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-[[2ygi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylocystis_hirsuta Methylocystis hirsuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGI OCA].
+<div class="pdbe-citations 2ygi" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Methylocystis hirsuta]]
-[[Category: Basle, A.]]
+[[Category: Basle A]]
-[[Category: Dennison, C.]]
+[[Category: Dennison C]]
-[[Category: Firbank, S J.]]
+[[Category: Firbank SJ]]
-[[Category: Ghazouani, A.]]
+[[Category: Ghazouani A]]
-[[Category: Gray, J.]]
+[[Category: Gray J]]
-[[Category: Metal transport]]
-[[Category: Methanotroph]]