3ku9: Difference between revisions

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[[Image:3ku9.jpg|left|200px]]


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==X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine==
The line below this paragraph, containing "STRUCTURE_3ku9", creates the "Structure Box" on the page.
<StructureSection load='3ku9' size='340' side='right'caption='[[3ku9]], [[Resolution|resolution]] 3.20&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'>[[3ku9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KU9 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]] 3.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr>
{{STRUCTURE_3ku9|  PDB=3ku9  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ku9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ku9 OCA], [https://pdbe.org/3ku9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ku9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ku9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ku9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAO1_MAIZE PAO1_MAIZE] Flavoenzyme involved in polyamine back-conversion (PubMed:16331971, Ref.4). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:16331971, Ref.4). Plays an important role in the regulation of polyamine intracellular concentration (Probable).<ref>PMID:16331971</ref> <ref>PMID:16331971</ref> <ref>PMID:16331971</ref>  


===X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine===
==See Also==
 
*[[Polyamine oxidase|Polyamine oxidase]]
 
== References ==
==About this Structure==
<references/>
3KU9 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KU9 OCA].
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Fiorillo, A.]]
[[Category: Fiorillo A]]
[[Category: Ilari, A.]]
[[Category: Ilari A]]
[[Category: Tavladoraki, P.]]
[[Category: Tavladoraki P]]
[[Category: Disulfide bond]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Glycoprotein]]
[[Category: Oxidoreductase]]
[[Category: Polyamine oxidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:40:15 2010''

Latest revision as of 05:02, 21 November 2024

X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermineX-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine

Structural highlights

3ku9 is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAO1_MAIZE Flavoenzyme involved in polyamine back-conversion (PubMed:16331971, Ref.4). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:16331971, Ref.4). Plays an important role in the regulation of polyamine intracellular concentration (Probable).[1] [2] [3]

See Also

References

  1. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
  2. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
  3. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i

3ku9, resolution 3.20Å

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