2o07

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:12, 28 December 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2o07.jpg|left|200px]]<br /><applet load="2o07" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2o07, resolution 1.89&Aring;" />
 
-
'''Human spermidine synthase'''<br />
 
-
==Overview==
+
==Human spermidine synthase==
 +
<StructureSection load='2o07' size='340' side='right'caption='[[2o07]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2o07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O07 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]] 1.89&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></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=2o07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o07 OCA], [https://pdbe.org/2o07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o07 RCSB], [https://www.ebi.ac.uk/pdbsum/2o07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o07 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SPEE_HUMAN SPEE_HUMAN] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine.
 +
== 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/o0/2o07_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=2o07 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.
Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.
-
==About this Structure==
+
Structure and mechanism of spermidine synthases.,Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781<ref>PMID:17585781</ref>
-
2O07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SPD:'>SPD</scene> and <scene name='pdbligand=MTA:'>MTA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O07 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structure and mechanism of spermidine synthases., Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN, Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17585781 17585781]
+
</div>
-
[[Category: Homo sapiens]]
+
<div class="pdbe-citations 2o07" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Spermidine synthase]]
+
-
[[Category: Arrowsmith, C H.]]
+
-
[[Category: Bochkarev, A.]]
+
-
[[Category: Edwards, A M.]]
+
-
[[Category: Loppnau, P.]]
+
-
[[Category: Min, J.]]
+
-
[[Category: Plotnikov, A N.]]
+
-
[[Category: SGC, Structural Genomics Consortium.]]
+
-
[[Category: Sundstrom, M.]]
+
-
[[Category: Weigelt, J.]]
+
-
[[Category: Wu, H.]]
+
-
[[Category: Zeng, H.]]
+
-
[[Category: MTA]]
+
-
[[Category: SPD]]
+
-
[[Category: sgc]]
+
-
[[Category: spermidine synthase]]
+
-
[[Category: structural genomics]]
+
-
[[Category: structural genomics consortium]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:59 2008''
+
==See Also==
 +
*[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Arrowsmith CH]]
 +
[[Category: Bochkarev A]]
 +
[[Category: Edwards AM]]
 +
[[Category: Loppnau P]]
 +
[[Category: Min J]]
 +
[[Category: Plotnikov AN]]
 +
[[Category: Sundstrom M]]
 +
[[Category: Weigelt J]]
 +
[[Category: Wu H]]
 +
[[Category: Zeng H]]

Current revision

Human spermidine synthase

PDB ID 2o07

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o07"
Personal tools