This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5zy8

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of C terminal truncated HadBC (3R-Hydroxyacyl-ACP Dehydratase) complex from Mycobacterium tuberculosis

Structural highlights

5zy8 is a 4 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.899Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Y637_MYCTU

Publication Abstract from PubMed

Comprehending the molecular strategies employed by Mycobacterium tuberculosis (Mtb) in FAS-II regulation is of paramount significance in order to curb tuberculosis (TB) progression. Mtb employs two sets of dehydratases, namely HadAB and HadBC (beta-hydroxy acyl ACP dehydratase), for the regulation of the Fatty Acid Synthase (FAS-II) pathway. We have utilized the Sequence similarity network (SSN) to comprehend the presence of two copies of the dehydratase gene in Mtb. This analysis groups HadC and HadA in different clusters, which could be attributed to the variability in their physiological role with respect to the acyl chain uptake. Our study reveals structural details pertaining to the crystal structure of the last remaining enzyme of the FAS-II pathway. It provides insights into the highly flexible hot-dog helix (alpha-HD) and substrate regulatory loop. Additionally, mutational studies assisted in establishing the role of the C-terminal end in HadC of HadBC in the regulation of Acyl Carrier Protein (AcpM) mediated interactions. Complemented with SPR and MD simulation studies, this work provides the first evidence of the molecular mechanisms involved in the differential binding affinity of the AcpM towards both mtbHadAB and mtbHadBC.

The C-terminal end of mycobacterial HadBC regulates AcpM interaction during the FAS-II pathway: a structural perspective.,Singh BK, Biswas R, Bhattacharyya S, Basak A, Das AK FEBS J. 2022 Feb 17. doi: 10.1111/febs.16405. PMID:35175661^[1]

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

References

↑ Singh BK, Biswas R, Bhattacharyya S, Basak A, Das AK. The C-terminal end of mycobacterial HadBC regulates AcpM interaction during the FAS-II pathway: a structural perspective. FEBS J. 2022 Feb 17. doi: 10.1111/febs.16405. PMID:35175661 doi:http://dx.doi.org/10.1111/febs.16405

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5zy8"

@@ Line 3: / Line 3: @@
 <StructureSection load='5zy8' size='340' side='right'caption='[[5zy8]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5zy8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZY8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5zy8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZY8 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0637, MTCY20H10.18 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), LH57_03445 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.899&#8491;</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=5zy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zy8 OCA], [https://pdbe.org/5zy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zy8 RCSB], [https://www.ebi.ac.uk/pdbsum/5zy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zy8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Y637_MYCTU Y637_MYCTU]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Myctu]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Basak, A]]
+[[Category: Basak A]]
-[[Category: Bhattacharyya, S]]
+[[Category: Bhattacharyya S]]
-[[Category: Biswas, R]]
+[[Category: Biswas R]]
-[[Category: Das, A K]]
+[[Category: Das AK]]
-[[Category: Singh, B K]]
+[[Category: Singh BK]]
-[[Category: Complex]]
-[[Category: Dehydratase]]
-[[Category: Heterodimer]]
-[[Category: Hot-dog fold]]
-[[Category: Lyase]]

5zy8

From Proteopedia

Current revision

Crystal structure of C terminal truncated HadBC (3R-Hydroxyacyl-ACP Dehydratase) complex from Mycobacterium tuberculosis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox