1eo1: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eo1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EO1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eo1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EO1 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eiw|1eiw]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eiw|1eiw]]</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=1eo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1eo1 PDBsum], [http://www.topsan.org/Proteins/NESGC/1eo1 TOPSAN]</span></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=1eo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1eo1 PDBsum], [http://www.topsan.org/Proteins/NESGC/1eo1 TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== 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: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Arrowsmith, C H | [[Category: Arrowsmith, C H]] | ||
[[Category: Cort, J R | [[Category: Cort, J R]] | ||
[[Category: Kennedy, M A | [[Category: Kennedy, M A]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Mixed a/b protein]] | [[Category: Mixed a/b protein]] | ||
[[Category: Mixed beta sheet]] | [[Category: Mixed beta sheet]] | ||
[[Category: Nesg]] | [[Category: Nesg]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Strand order 321456]] | [[Category: Strand order 321456]] | ||
[[Category: Strands 2 and 6 antiparallel to rest | [[Category: Strands 2 and 6 antiparallel to rest]] | ||
Revision as of 23:15, 22 December 2014
Solution structure of hypothetical protein MTH1175 from Methanobacterium thermoautotrophicumSolution structure of hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium thermoautotrophicum has been determined by NMR spectroscopy. MTH1175 is part of a family of conserved hypothetical proteins (COG1433) with unknown functions which contains multiple paralogs from all complete archaeal genomes and the archaeal gene-rich bacterium Thermotoga maritima. Sequence similarity indicates this protein family may be related to the nitrogen fixation proteins NifB and NifX. MTH1175 adopts an alpha/beta topology with a single mixed beta-sheet, and contains two flexible loops and an unstructured C-terminal tail. The fold resembles that of Ribonuclease H and similar proteins, but differs from these in several respects, and is not likely to have a nuclease activity. NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.,Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA J Struct Funct Genomics. 2000;1(1):15-25. PMID:12836677[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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