2cmh
From Proteopedia
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| - | {{STRUCTURE_2cmh| PDB=2cmh | SCENE= }} | ||
| - | ===Crystal Structure of Spermidine Synthase from Helicobacter Pylori=== | ||
| - | {{ABSTRACT_PUBMED_17357156}} | ||
| - | == | + | ==Crystal Structure of Spermidine Synthase from Helicobacter Pylori== |
| - | [[http://www.uniprot.org/uniprot/SPEE_HELPY SPEE_HELPY | + | <StructureSection load='2cmh' size='340' side='right'caption='[[2cmh]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2cmh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CMH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=2cmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cmh OCA], [https://pdbe.org/2cmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cmh RCSB], [https://www.ebi.ac.uk/pdbsum/2cmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cmh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SPEE_HELPY SPEE_HELPY] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.<ref>PMID:16009566</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/2cmh_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2cmh ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine during spermidine biosynthesis. Helicobacter pylori PAPT (HpPAPT) has a low sequence identity with other PAPTs and lacks the signature sequence found in other PAPTs. The crystal structure of HpPAPT, determined by multiwavelength anomalous dispersion, revealed an N-terminal beta-stranded domain and a C-terminal Rossmann-like domain. Structural comparison with other PAPTs showed that HpPAPT has a unique binding pocket between two domains, numerous non-conserved residues, a less acidic electrostatic surface potential, and a large buried space within the structure. HpPAPT lacks the gatekeeping loop that facilitates substrate binding in other PAPTs. PAPTs are essential for bacterial cell viability; thus, HpPAPT may be a potential antimicrobial drug target for H. pylori owing to its characteristic PAPT sequence and distinct conformation. | ||
| - | + | Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-like fold with a distinct active site.,Lu PK, Tsai JY, Chien HY, Huang H, Chu CH, Sun YJ Proteins. 2007 May 15;67(3):743-54. PMID:17357156<ref>PMID:17357156</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 2cmh" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]] | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Lu | + | __TOC__ |
| - | [[Category: Sun | + | </StructureSection> |
| - | + | [[Category: Helicobacter pylori 26695]] | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Lu P-K]] | |
| - | + | [[Category: Sun Y-J]] | |
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Current revision
Crystal Structure of Spermidine Synthase from Helicobacter Pylori
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