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4a22

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Revision as of 13:10, 5 August 2016

STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE BOUND TO N-(4-HYDROXYBUTYL)-GLYCOLOHYDROXAMIC ACID BIS-PHOSPHATE

Structural highlights

4a22 is a 4 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	4a21
Activity:	Fructose-bisphosphate aldolase, with EC number 4.1.2.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALF_MYCTU] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity).

Publication Abstract from PubMed

The search for anti-TB drugs active against persistent bacilli has led to our interest in metallo-dependent class II fructose-1,6-bisphosphate aldolase (FBA-tb), a key enzyme of gluconeogenesis absent from mammalian cells. Knock-out experiments at the fba-tb locus indicated that this gene is required for the growth of M. tb on gluconeogenetic substrates and in glucose-containing medium. Surface labeling and enzymatic activity measurements revealed that this enzyme is exported to the cell surface of M. tb and is produced under various axenic growth conditions including oxygen depletion, and hence by non-replicating bacilli. Importantly, FBA-tb is also produced in vivo in the lungs of infected guinea pigs and mice. FBA-tb binds human plasmin(ogen) and protects FBA-tb-bound plasmin from regulation by alpha-2-antiplasmin, suggestive of an involvement of this enzyme in host-pathogen interactions. The crystal structures of FBA-tb in the native form and in complex with a hydroxamate substrate analog were determined to 2.35 and 1.9 angstroms resolution, respectively. Whereas inhibitor attachment had no effect on the plasminogen-binding activity of FBA-tb, it competed with the natural substrate of the enzyme, fructose-1,6-bisphosphate, and substantiated a previously unknown reaction mechanism associated with metallo-dependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding. Altogether, our results highlight the potential of FBA-tb as a novel therapeutic target against both replicating and non-replicating bacilli.

Glycolytic and non-glycolytic functions of the fructose-1,6-bisphosphate aldolase of Mycobacterium tuberculosis, an essential enzyme produced by replicating and non-replicating bacilli.,Santangelo MD, Gest PM, Guerin ME, Coincon M, Pham H, Ryan G, Puckett SE, Spencer JS, Gonzalez-Juarrero M, Daher R, Lenaerts AJ, Schnappinger D, Therisod M, Ehrt S, Sygusch J, Jackson M J Biol Chem. 2011 Sep 23. PMID:21949126^[1]

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

References

↑ Santangelo MD, Gest PM, Guerin ME, Coincon M, Pham H, Ryan G, Puckett SE, Spencer JS, Gonzalez-Juarrero M, Daher R, Lenaerts AJ, Schnappinger D, Therisod M, Ehrt S, Sygusch J, Jackson M. Glycolytic and non-glycolytic functions of the fructose-1,6-bisphosphate aldolase of Mycobacterium tuberculosis, an essential enzyme produced by replicating and non-replicating bacilli. J Biol Chem. 2011 Sep 23. PMID:21949126 doi:10.1074/jbc.M111.259440

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a22"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE BOUND TO N-(4-HYDROXYBUTYL)-GLYCOLOHYDROXAMIC ACID BIS-PHOSPHATE==
 <StructureSection load='4a22' size='340' side='right' caption='[[4a22]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a22]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A22 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a22]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A22 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TD4:4-{HYDROXY[(PHOSPHONOOXY)ACETYL]AMINO}BUTYL+DIHYDROGEN+PHOSPHATE'>TD4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a21|4a21]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a22 RCSB], [http://www.ebi.ac.uk/pdbsum/4a22 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a22 OCA], [http://pdbe.org/4a22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a22 RCSB], [http://www.ebi.ac.uk/pdbsum/4a22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a22 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4a22" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 28: @@
 </StructureSection>
 [[Category: Fructose-bisphosphate aldolase]]
-[[Category: Mycobacterium tuberculosis]]
 [[Category: Coincon, M]]
 [[Category: Daher, R]]

4a22

From Proteopedia

Revision as of 13:10, 5 August 2016

STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE BOUND TO N-(4-HYDROXYBUTYL)-GLYCOLOHYDROXAMIC ACID BIS-PHOSPHATE

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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