1b37

From Proteopedia

(Difference between revisions)

Current revision

A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE

Structural highlights

1b37 is a 3 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 1.9Å
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]

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 PubMed

BACKGROUND: Polyamines are essential for cell growth and differentiation; compounds interfering with their metabolism are potential anticancer agents. Polyamine oxidase (PAO) plays a central role in polyamine homeostasis. The enzyme utilises an FAD cofactor to catalyse the oxidation of the secondary amino groups of spermine and spermidine. RESULTS: The first crystal structure of a polyamine oxidase has been determined to a resolution of 1.9 Angstroms. PAO from Zea mays contains two domains, which define a remarkable 30 Angstrom long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel. CONCLUSIONS: PAO specifically oxidizes substrates that have both primary and secondary amino groups. The complex with MDL72527 shows that the primary amino groups are essential for the proper alignment of the substrate with respect to the flavin. Conservation of an N-terminal sequence motif indicates that PAO is member of a novel family of flavoenzymes. Among these, monoamine oxidase displays significant sequence homology with PAO, suggesting a similar overall folding topology.

A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.,Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A Structure. 1999 Mar 15;7(3):265-76. PMID:10368296^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A. A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure. 1999 Mar 15;7(3):265-76. PMID:10368296

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b37"

@@ Line 1: / Line 1: @@
-[[Image:1b37.gif|left|200px]]
-<!--
+==A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE==
-The line below this paragraph, containing "STRUCTURE_1b37", creates the "Structure Box" on the page.
+<StructureSection load='1b37' size='340' side='right'caption='[[1b37]], [[Resolution|resolution]] 1.90&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'>[[1b37]] is a 3 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=1B37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B37 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]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_1b37|  PDB=1b37  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b37 OCA], [https://pdbe.org/1b37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b37 RCSB], [https://www.ebi.ac.uk/pdbsum/1b37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b37 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>
+== 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/b3/1b37_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1b37 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: Polyamines are essential for cell growth and differentiation; compounds interfering with their metabolism are potential anticancer agents. Polyamine oxidase (PAO) plays a central role in polyamine homeostasis. The enzyme utilises an FAD cofactor to catalyse the oxidation of the secondary amino groups of spermine and spermidine. RESULTS: The first crystal structure of a polyamine oxidase has been determined to a resolution of 1.9 Angstroms. PAO from Zea mays contains two domains, which define a remarkable 30 Angstrom long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel. CONCLUSIONS: PAO specifically oxidizes substrates that have both primary and secondary amino groups. The complex with MDL72527 shows that the primary amino groups are essential for the proper alignment of the substrate with respect to the flavin. Conservation of an N-terminal sequence motif indicates that PAO is member of a novel family of flavoenzymes. Among these, monoamine oxidase displays significant sequence homology with PAO, suggesting a similar overall folding topology.
-'''A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE'''
+A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.,Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A Structure. 1999 Mar 15;7(3):265-76. PMID:10368296<ref>PMID:10368296</ref>
-==Overview==
-BACKGROUND: Polyamines are essential for cell growth and differentiation; compounds interfering with their metabolism are potential anticancer agents. Polyamine oxidase (PAO) plays a central role in polyamine homeostasis. The enzyme utilises an FAD cofactor to catalyse the oxidation of the secondary amino groups of spermine and spermidine. RESULTS: The first crystal structure of a polyamine oxidase has been determined to a resolution of 1.9 Angstroms. PAO from Zea mays contains two domains, which define a remarkable 30 Angstrom long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel. CONCLUSIONS: PAO specifically oxidizes substrates that have both primary and secondary amino groups. The complex with MDL72527 shows that the primary amino groups are essential for the proper alignment of the substrate with respect to the flavin. Conservation of an N-terminal sequence motif indicates that PAO is member of a novel family of flavoenzymes. Among these, monoamine oxidase displays significant sequence homology with PAO, suggesting a similar overall folding topology.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-B37 is a [[Single protein]] structure of sequence 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=1B37 OCA].
+</div>
+<div class="pdbe-citations 1b37" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase., Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A, Structure. 1999 Mar 15;7(3):265-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10368296 10368296]
+*[[Polyamine oxidase|Polyamine oxidase]]
-[[Category: Polyamine oxidase]]
+== References ==
-[[Category: Single protein]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Zea mays]]
-[[Category: Angelini, R.]]
+[[Category: Angelini R]]
-[[Category: Ascenzi, P.]]
+[[Category: Ascenzi P]]
-[[Category: Binda, C.]]
+[[Category: Binda C]]
-[[Category: Coda, A.]]
+[[Category: Coda A]]
-[[Category: Federico, R.]]
+[[Category: Federico R]]
-[[Category: Mattevi, A.]]
+[[Category: Mattevi A]]
-[[Category: Flavin-dependent amine oxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:00:07 2008''

1b37

From Proteopedia

Current revision

A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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