1am2: Difference between revisions

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 <StructureSection load='1am2' size='340' side='right'caption='[[1am2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1am2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_xenopei"_(sic)_schwabacher_1959 "mycobacterium xenopei" (sic) schwabacher 1959]. The November 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Inteins''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_11 10.2210/rcsb_pdb/mom_2010_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1AM2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1am2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_xenopi Mycobacterium xenopi]. The November 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Inteins''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_11 10.2210/rcsb_pdb/mom_2010_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AM2 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1789 "Mycobacterium xenopei" (sic) Schwabacher 1959])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1am2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am2 OCA], [http://pdbe.org/1am2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1am2 RCSB], [http://www.ebi.ac.uk/pdbsum/1am2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1am2 ProSAT]</span></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=1am2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am2 OCA], [https://pdbe.org/1am2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1am2 RCSB], [https://www.ebi.ac.uk/pdbsum/1am2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1am2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GYRA_MYCXE GYRA_MYCXE]] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity).
+[https://www.uniprot.org/uniprot/GYRA_MYCXE GYRA_MYCXE] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1am2 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Several genes from prokaryotes and lower eukaryotes have been found to contain an in-frame open reading frame, which encodes for an internal protein (intein). Post-translationally, the internal polypeptide auto-splices and ligates the external sequences to yield a functional external protein (extein) and an intein. Most, but not all inteins, contain, apart from a splicing domain, a separate endonucleolytic domain that enables them to maintain their presence by a homing mechanism. We report here the crystal structure of an intein found in the gyrase A subunit from Mycobacterium xenopi at 2.2 A resolution. The structure contains an unusual beta-fold with the catalytic splice junctions at the ends of two adjacent antiparallel beta-strands. The arrangement of the active site residues Ser 1, Thr 72, His 75, His 197, and Asn 198 is consistent with a four-step mechanism for the cleavage-ligation reaction. Using site-directed mutagenesis, the N-terminal cysteine, proposed as the nucleophile in the first step of the splicing reaction, was changed to a Ser 1 and Ala 0, thus capturing the intein in a pre-spliced state.
-Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing.,Klabunde T, Sharma S, Telenti A, Jacobs WR Jr, Sacchettini JC Nat Struct Biol. 1998 Jan;5(1):31-6. PMID:9437427<ref>PMID:9437427</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1am2" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Inteins]]
 [[Category: Large Structures]]
+[[Category: Mycobacterium xenopi]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Klabunde, T]]
+[[Category: Klabunde T]]
-[[Category: Sacchettini, J C]]
+[[Category: Sacchettini JC]]
-[[Category: Sharma, S]]
+[[Category: Sharma S]]
-[[Category: Intein]]
-[[Category: Protein splicing]]